ACYLATED OLIGOPEPTIDE DERIVATIVES HAVING CELL SIGNAL INHIBITING ACTIVITY

Abstract: The invention relates to an acylated peptide, namely a compound of formula (I), wherein n is 0 to 15, X is arylcarbonyl, cycloalkylcarbonyl, tricycloalkylcarbonyl, arylsulfonyl, heterocyclylcarbonyl, heterocyclylsulfonyl, carbamoyl-lower alkanoyl, aryl-lower alkylcarbonyl, cycloalkyl-lower alkylcarbonyl, aryl-lower alkylsulfonyl, heterocyclyl-lower alkylcarbonyl, heterocyclyl-lower alkylsulfonyl with the proviso that in any of the lower alkyl radicals mentioned a methylene group may be replaced with oxa, aza or thia; heterocyclyl-lower alkenylcarbonyl or aryl-lower alkenylcarbonyl; or, if Y is a secondary or tertiary amino group, is one of the moieties X mentioned above or lower alkanoyl, halo-lower alkanoyl, lower-alkoxycarbonyl, aryl-lower alkoxycarbonyl or cycloalkyl-lower alkoxycarbonyl; PTI is the bivalent radical of tyrosine or (preferably) the bivalent radical of phosphotyrosine or a phosphotyrosine mimic, AA stands for a bivalent radical of a natural or unnatural amino acid, and Y is hydroxy, a C-terminal protecting group or a primary, secondary or tertiary amino group, or a salt thereof, said compound being useful for the treatment of diseases that respond to inhibition of the interaction of (a) protein(s) comprising (an) SH2 domain(s) and a protein tyrosine kinase or a modified version thereof.

Description: * ACYLATED OLIGOPEPTIDE DERIVATIVES HAVING CELL SIGNAL INHIBITING ACTIVITY f The present invention relates to pharmaceutically active compounds comprising a N-acyl peptide structure, processes for the preparation of said compounds, pharmaceutical preparations comprising said compounds, the compounds for the use in the therapeutic (including prophylactic) or diagnostic treatment of the animal or especially human body, and the use of said compounds for the therapeutic or diagnostic treatment of the animal or especially human body or for the manufacture of pharmaceutical preparations. Background of the invention The search for new classes of compounds for the therapy and prophylaxis of proliferative diseases, cancer and metabolic deregulation is one of the most important tasks for pharmaceutical research. These diseases affect a large portion of the population, leading to suffering and often being the cause for the death of the individuals stricken therewith. Signal transduction is the process of relaying extracellular messages, e.g. chemical messages in the form of growth factors, hormones and neurotransmitters, via receptors, e.g. cell-surface receptors, to the interior of the cell. At the heart of this biological communication are the protein-tyrosine kinases. These enzymes, found, for example, as either transmembrane growth factor receptors or as nuclear or cytosolic non-receptor proteins, catalyze the phosphorylation of specific tyrosine residues. This class of enzymes includes, but is not limited to, the PDGF receptor, the FGF receptor, the HGF receptor, members of the EGF receptor family such as the EGF receptor, erb-B2, erb-B3 and erb-B4, the src kinase family, Fak kinase and the Jak kinase family. The tyrosine-phosphorylated proteins are involved in a range of metabolic processes, from proliferation and growth to differentiation. Protein-tyrosine phosphorylation is known to be involved in modulating the activity of some target enzymes as well as in generating specific complex networks involved in signal transduction via various proteins containing a specific amino acid sequence called * a Src Homology Region or SH2 domain (for review see Proc. Natl. Acad. Sci. USA 90, 5891 * (1990)). A malfunction in this protein-tyrosine phosphorylation through tyrosine kinase - overexpression or deregulation is manifested by various oncogenic and (hyper-) proliferative disorders such as cancer, inflammation, autoimmune disease, hyperproliferative skin disorders, such as psoriasis, and allergy/asthma. SH2- and/or SH3-comprising proteins that play a role in cellular signaling and transforma¬ tion include, but are not limited to, the following: Src, Lck, Fps, ras GTPase-activating protein (GAP), phospholipase C, phosphoinositol-3 (PI-3) kinase, Fyn, Lyk, Fgr, Fes, ZAP- 70, Sem-5, p85, SHPTP1 , SHPTP2, corkscrew, Syk, Lyn, Yes, Hck, Dsrc, Tec, Atk/Bpk, Itk/Tsk, Arg, Csk, tensin, Vav, Emt, Grb2, BCR-Abl, She, Nek, Crk, CrkL, Syp, Blk, 113TF, 91 TF, Tyk2, JAK1 , and JAK2, especially Src, phosholipase C, phosphoinositol-3 (PI-3) kinase, Grb2, BCR-Abl, She, Nek, Crk and CrkL. A direct link has been established between activated receptor kinases and Ras with the finding that the mammalian Grb2 protein, a 26 kilodalton protein comprising a single SH2 and two SH3 domains, directly couples receptor tyrosine kinases to the Ras guanine nucleotide exchange factor Sos in mammals and also Drosophila. The Grb2 SH2 domain binds to specific tyrosine phosphorylated sequences, e.g. in receptor tyrosine kinases, while the Grb2 SH3 domains bind to proline-rich sequences present in the Sos exchange factor. The significance of ras-regulatory proteins in human tumors is also highlighted by the critical role of GRB2 in BCR-Abl mediated oncogenesis (J. Exp. Med., 179(1). 167-175 (1994)). Recently, DNA sequences within the chromosomal locus 17q22-qter, which harbors the GRB2 gene, were shown by comparative genomic hybridization to exhibit a high frequency of amplification in both human breast cancer cell lines and tumors (Proc. Natl. Acad. Sci. USA 91, 2156-2160 (1994)). In a study of GRB2 gene expression in human breast cancer cell lines, Northern Blot analysis also revealed that 7/19 breast cancer cell lines exhibited more than 2 fold overexpression of GRB2 mRNA relative to normal breast epithelial cells. In MCF-7, MDA- MB-361 , and -453 cells, the overexpression of GRB2 mRNA was accompanied by a 10-20 fold increase in the amount of GRB2 protein (Oncogene 9, 2723 (1994)). SH2 domains represent recognition motifs for specific tyrosine-phosphorylated peptide sequences. Short, conserved motifs, primarily 3 to 6 amino acids on the carboxy-terminal side of a phosphotyrosine residue, carry the sequence-specific information for SH2- recognition. This concept has been supported by the mapping of separate sites for binding of SH2 domains from different signalling molecules on various receptors [see, e.g., Cell 69, 413 (1992); Proc. Natl. Acad. Sci. USA 89, 678 (1992); Mol. Cell. Biol. tg, 991 (1992); EMBO J. JJ . , 1365 (1992); EMBO J. H, 559 (1992); EMBO J. H, 3911 (1992); Cell 73, 321 (1993)]. Degenerate peptide libraries have also been used to predict the specifity of individual SH2 domains (src family members, Abl, Nek, Sem5, phosholipase C-γ, p85 subunit of PI-3 kinase, and HCP (amino terminal SH2) [see Cell 72, 767 (1993); Mol. Cell. Biol. 14, 2777 (1994)]). High-resolution crystallographic analysis and nuclear magnetic resonance of the SH2 domains of Src, Lck, PLC-γ C-terminal, p85 N-terminal, Abl, Syp C- terminal have also revealed that the region on the carboxyl side of the phosphotyrosine carries the sequence-specific information for SH2 recognition. Each of these SH2 containing proteins controls a cellular pathway involved in the biological response to a growth factor. Activation of a particular pathway can thus be inhibited by designing a small molecule that specifically disrupts a phosphoprotein/SH2 domain interaction. The approach of selectively eliminating a mitogenic pathway by a point mutation of the tyrosine kinase or a tyrosine-phosphorylated protein has been successful. For example, tyrosine 317 is the major site for SHC tyrosine phosphorylation and is the sole high-affinity binding site for Grb2 SH2. Mutant SHC proteins with substitution of tyrosine 317 by phenylalanine loose the capacity to be highly phosphorylated on tyrosine upon growth factor activation, to bind Grb2 and to induce neoplastic transformation [see Oncogene 9, 2827 (1994)]. An FGR receptor with a point mutation at tyrosine 766 does not bind phospholipase C-γ (an SH2-containing protein). It abolishes phosphatidylinositol turnover and calcium flux but not mitogenesis [see Nature 358, 678 (1992)]. For Epidermal Growth Factor Receptor (EGFR) it has been shown that tyrosine 1068 is the binding site for Grb2 SH2 (see Buday et al., Cell 73, 611-620 (1993)). A phosphopeptide based on the surrounding sequence, Pro-Val-Pro-Glu-Tyr(PO 3 H 2 )-lle-Asn-Gln-Ser, was shown to inhibit the interaction of phosphorylated EGFR and Grb2. It has also been demonstrated that uncoupling a tyrosine kinase from signal transduction pathways results therapeutically in antitumor activity. Antitumor activity for tyrosine kinase inhibitors has been demonstrated both in vitro and in vivo [see J. Antibiot. 39, 170 (1986); Eur. J. Cancer 26(6), 722 (1990); J. Med. Chem. 34, 2328 (1991); Cancer Res. 51, 4430 (1991); J. Med. Chem. 34, 2328 (1991); Helv. Chim. Acta 75, 696 (1992); Cancer Res. 52, 4492 (1992); Science 265, 1093 (1994); Science 267. 1782 (1995)]. For example, it has been shown that a small molecule called PD 153035 rapidly suppressed autophosphoryla¬ tion of the EGF receptor at low concentrations in human epidermoid carcinoma cells and selectively blocked EGF-mediated cellular processes including mitogenesis, early gene expression and oncogenic transformation [see Science 265, 1093 (1994)]. In addition, it has been shown that tyrosine kinase inhibitors RS-13022 and 14620 supressed EGF-stimulated proliferation of HER-14 cells (transfected NIH 3T3 cells) and MH-85 cells in vitro. The MH- 85 tumor is a human squamous cell carcinoma associated with three paraneoplastic syndromes: hypercalcemia, leukocytosis and cachexia. The well-characterized cells show overexpression of endogenous EGF receptor tyrosine kinase and are dependent on the EGF receptor signal transduction pathway for growth in vitro and in nude mice. In vivo, the compounds suppressed the growth of MH-85 tumors in nude mice as well as the expression of the paraneoplastic syndromes. An increase in life span of 75% was observed for RG- 13022-treated tumor bearing mice [see Cancer Res. 51, 4430 (1991)]. 4,5-Dianilinophthalimides inhibit the growth of human tumor cells that overexpress EGFR or HER2-ErbB2 and exhibit good antitumor activity in mice in which these tumors are grown as xenografts (see Buchdunger et al., Proc. Natl. Acad. Sci USA 91, 2334 (1994) and Trinks et al., J. Med. Chem. 37, 1015 (1994)). Immunologic downregulation of the p185 neu receptor in transgenic mice that express the rat neu oncogene (neuT) in mammary epithelial cells can also effectively prevent breast tumor development (Nature Medecine, 1 (7), 1995). Anilinoquinazolines also represent a class of compounds which exhibit promising anti¬ cancer activity. They were shown to inhibit the EGF-stimulated growth of human KB nasopharyngeal cells in vitro at concentrations of 1 -10 μM. These results show that the inhibition of regulatory pathways by way of inhibition of protein tyrosine kinases results in therapeutically useful effects. It is therefore reasonable that inhibition at the level of interaction of protein tyrosine kinases with other, e.g. regulatory, proteins, for example those with SH2 domains, will result in similar therapeutic usefulness. Not all phosphoproteins bind the same SH2-binding proteins. The divergent residues of individual domains can be shown to confer specificity for binding to structural variants within each ligand binding site [for SH2 domains, ligands with different amino acids surrounding the respective phosphotyrosine residue]. Various synthetic peptides derived from these ligand binding sites and as small as five amino acids in length have been shown to interfere specifically with these interactions in vitro [Mol. Cell. Biol. H(2), 1125 (1991); Mol. Cell. Biol. 12(4), 1451 (1992); Cell 69, 413 (1992); and Cell Z2, 767-778 (1993)] It is a goal of the present invention to present small organic molecules that, due to their ability to mimic the structure of the phosphotyrosine peptide binding site, have the ability to disrupt the interaction between SH2 domains of (e.g. regulatory) proteins, for example that of Grb2, and proteins with phosphorylated moieties, especially phosphorylated tyrosine moieties, for example phosphorylated protein tyrosine kinase receptors. The effect is to inhibit the association of SH2 containing (e.g. regulatory) proteins with a protein tyrosine kinase in order to inhibit downstream signalling through one or more specifically targeted effector proteins. Summary of the Invention Surprisingly, it has been found that the compounds of the present invention show very favourable and valuable characteristics for pharmaceutical application, especially with regard to the therapeutic (including, in a broader sense, prophylactic) and/or diagnostic treatment of diseases that depend on the downstream signal transduction pathways, especially those mediated by an interaction of a protein comprising a SH2 domain with a tyrosine phosphorylated protein, such as a phosphorylated tyrosine protein kinase; proteins comprising one or more SH2 domains that are effective in cellular signalling and transformation include, but are not limited to, the following: Src, Lck, Fps, ras GTPase- activating protein (GAP), phospholipase C, phosphoinositol-3 (PI-3) kinase, Fyn, Lyk, Fgr, Fes, ZAP-70, Sem-5, p85, SHPTP1 , SHPTP2, corkscrew, Syk, Lyn, Yes, Hck, Dsrc, Tec, Atk/Bpk, Itk/Tsk, Arg, Csk, tensin, Vav, Emt, Grb2, BCR-Abl, She, Nek, Crk, CrkL, Syp, Blk, 113TF, 91 TF, Tyk2, JAK1 , and JAK2. Especially, very good inhibition is already found in vitro with the compounds of formula I. The new peptides of this invention preferably show selective inhibition of the binding of SH2-comprising proteins, such as Grb2, to phosphorylated proteins, especially activated growth factor receptor tyrosine kinases like EGF receptor tyrosine protein kinase, or She. The compounds of formula I disrupt the interaction between the SH2-comprising protein and the phosphoprotein, such as protein tyrosine kinase, and thus blocks the ability of the tyrosine protein kinases to initiate regulatory events depending on the SH2-comprising proteins, thus resulting in inhibition of specific downstream signal transduction pathways utilized in some hyperproliferative diseases, such as tumor diseases and psoriasis and the other diseases mentioned above and below, by uncoupling of the respective protein tyrosine kinase(s) from the respective SH2-containing effector protein. One feature of the present invention is the positive effect of the moieties X as defined below on the inhibitory action of the compounds of the present invention on the interaction of a broad variety of phosphoproteins, especially phosphotyrosine-comprising proteins, to SH2-comprising proteins (e.g. those mentioned below in the definition of the bivalent radical -(AA)n-). These moieties X are even able to allow for large sequence variability in the pep¬ tide derivatives of formula I. Many of the compounds of formula I show inhibition if n in for¬ mula I given below is 3, 2 and even 1 or 0. in addition, the C- and especially the N-terminal modification even allows that PTI in formula I given below is simply tyrosine without any phosphono group or an analogue thereof; even then very active compounds can be obtained. Detailed description of the invention The invention relates to an acylated peptide, namely a compound of the formula I, • (AA) n . PTI ' -Y (I) wherein n is 0 to 15, X is arylcarbonyl, cycloalkylcarbonyl, tricycloalkylcarbonyl, arylsulfonyl, heterocyclylcarbonyl, heterocyclylsulfonyl, carbamoyl-lower alkanoyl, aryl-lower alkylcarbonyl, cycloalkyl-lower alkylcarbonyl, aryl-lower alkylsulfonyl, heterocyclyl-lower alkylcarbonyl, heterocyclyl-lower alkylsulfonyl with the proviso that in any of the lower alkyl radicals mentioned a methylene group may be replaced with oxa, aza or thia; heterocyclyl-lower alkenylcarbonyl or aryl- lower-alkenylcarbonyl; or, if Y is a secondary or tertiary amino group, is one of the morieties X mentioned above or lower alkanoyl, halo-lower alkanoyl, lower-alkoxycarbonyl, aryl-lower alkoxycarbonyl or cycloalkyl-lower alkoxycarbonyl; PTI is the bivalent radical of tyrosine or (preferably) the bivalent radical of phosphotyrosine or a phosphotyrosine mimic, AA stands for a bivalent radical of a natural or unnatural amino acid, and Y is hydroxy, a C-terminal protecting group or a primary, secondary or tertiary amino group, or a salt thereof. Unless indicated otherwise, the general terms and names used in the description of the present invention preferably have the following meanings: The term "lower" defines a moiety with up to and including maximally 7, especially up to and including maximally 4, carbon atoms, said moiety being branched or straight-chained. Lower alkyl, for example, is methyl, ethyl, n-propyl, sec-propyl, n-butyl, isobutyl, sec-butyl, tert¬ butyl, n-pentyl, n-hexyl or n-heptyl. In the case of lower alkenyl, the term "lower" designates a residue with 2 to 7 carbon atoms, preferably with 2 to 4 carbon atoms, such as vinyl, allyl or 1 - or 2-butenyl. The compounds of formula I with one or more centers of asymmetry, such as one or more asymmetric carbon atoms, may be present in the form of isomeric mixtures or pure isomers; for example, a compound of formula I with one center of asymmetry may be present in the form of a pure enantiomer or a mixture of enantiomers, e.g. a racemate, while a compound of formula I with two or more centers of asymmetry may be present in the form of a pure isomer (enantiomer) or in the form of diastereomeric mixtures, e.g. mixtures of epimers. A double bond in a compound of formula I may be present in the cis (Z) or trans (E) form. In a compound of formula I with a center of asymmetry and a double bond, the respective compound may be present as a mixture of isomers or as a pure isomer. Generally, pure isomers of compounds of formula I are preferred over isomeric mixtures. n is preferably 1 to 15, more preferably 1 to 4, even more preferably 1 to 3 and most preferably 2 or especially 3. Aryl has preferably from 6 to 14 ring carbon atoms, such as in phenyl (which is especially preferred), naphthyl (which is especially preferred), such as 1 -naphthyl or 2-naphthyl, indenyl, indanyl, anthryl, phenanthryl (which is especially preferred), acenaphthyl or fluorenyl (which is preferred), and may be unsubstituted or preferably mono- to tri¬ substituted, especially by amino, mono- or di-lower alkylamino, lower alkanoylamino, such as acetylamino, amino-lower alkyl, mono- or di-loweralkylamino-lower alkyl, lower alkanoyl- amino-lower alkyl, hydroxy, lower alkoxy, such as methoxy, carboxy, lower-alkoxycarbonyl, such as methoxycarbonyl, phenyl-, naphthyl- or fluorenyl-lower alkoxycarbonyl, such as benzyloxycarbonyl, lower alkanoyl, cyano, lower alkyl, for example methyl, ethyl or propyl, halo-lower alkyl, for example trifluoromethyl, phenyl, 1- or 2-naphthyl, halogen, for example fluorine, chlorine or bromine, mercapto, lower-alky Ith io, such as methylthio, lower alkyl-sul- finyl, such as methylsulfinyl (CH 3 -S(=O)-), sulfo, lower alkanesulfonyl, for example metha¬ nesulfonyl (CH 3 -S((O) 2 )-), carbamoyl, mono- or di-lower alkylcarbamoyl, sulfamoyl, mono- or di-lower alkylaminosulfonyl, and /or by nitro; more preferably substituted by one or two substituents selected independently from amino, mono- or di-lower alkylamino, lower alka¬ noylamino, such as acetylamino, amino-lower alkylamino, mono- or di-loweralkylamino-io- wer alkyl, lower alkanoylamino-lower alkyl, hydroxy, lower alkoxy, such as methoxy, carb¬ oxy, lower-alkoxycarbonyl, such as methoxycarbonyl, cyano, halogen, such as chloro or bromo, lower-alkylthio, such as methylthio, and lower alkyl-sulfinyl, such as methylsulfinyl (CH 3 -S(=O)-); most preferably mono- or disubstituted by amino or hydroxy. Cycloalkyl preferably has from 3 to 10 ring carbon atoms, preferably from 4 to 7 carbon atoms, and is unsubstituted or preferably mono- to tri-substituted, especially by amino, mono- or di-lower alkylamino, lower alkanoylamino, such as acetylamino, amino-lower alkyl, mono- or di-loweralkylamino-lower alkyl, lower alkanoylamino-lower alkyl, hydroxy, lower alkoxy, such as methoxy, carboxy, lower-alkoxycarbonyl, such as methoxycarbonyl, phenyl-, naphthyl- or fluorenyl-lower alkoxycarbonyl, such as benzyloxycarbonyl, lower alkanoyl, cyano, lower alkyl, for example methyl, ethyl or propyl, halo-lower alkyl, for example tri¬ fluoromethyl, phenyl, 1- or 2-naphthyl, halogen, for example fluorine, chlorine or bromine, mercapto, lower-alkylthio, such as methylthio, lower alkyl-sulfinyl, such as methylsulfinyl (CH 3 -S(=O)-), sulfo, lower alkanesulfonyl, for example methanesulfonyl (CH 3 -S((O) 2 )-), carbamoyl, mono- or di-lower alkylcarbamoyl, sulfamoyl, mono- or di-lower alkylamino- sulfonyl, and /or by nitro; more preferably mono- or di-substituted by a substituent selected independently from amino, mono- or di-lower alkylamino, lower alkanoylamino, such as ace¬ tylamino, amino-lower alkylamino, mono- or di-loweralkylamino-iower alkyl, lower alkanoyl¬ amino-lower alkyl, hydroxy, lower alkoxy, such as methoxy, carboxy, lower-alkoxycarbonyl, such as methoxycarbonyl, cyano, halogen, such as chloro, lower-alkylthio, such as methyl¬ thio, and lower alkyl-sulfinyl, such as methylsulfinyl (CH 3 -S(=O)-); most preferably mono- or disubstituted by amino. Cycloalkyl may also be annelated with a benzo ring, such as in 1 ,2,3,4-tetrahydronaphthyl. Tricycloalkyl preferably has 8 to 16 carbon atoms and is, for example, tricyclo[5.2.1.0 2,6 ]dec- 8-yl or especially adamantyl, preferably 1 -adamantyl. Heterocyclyl is preferably a single or double ring system having from 3 to 10 ring atoms, is bonded preferebly via a carbon atom or also via a nitrogen atom and contains up to 3 hetero atoms selected from oxygen, sulfur, sulfur linked to 1 or 2 oxygen atoms and, most preferably, nitrogen; which in addition may also be fused with 1 or 2 phenyl radicals or with 1 or 2 cycloalkyl radicals, cycloalkyl preferably having from 5 to 7 ring atoms; and which may be unsaturated or partially or fully saturated, for example thienyl, furyl, pyrrolyl, imid¬ azolyl, such as imidazole-4-yl, pyrazolyl, oxazolyl, thiazolyl, such as 4- or 5-thiazolyl, tetraz¬ olyl, pyridyl, such as pyridin-3- or pyridin-4-yl, pyrazinyl, such as pyrazin-2-yl, pyrimidinyl, py¬ ridazinyl, indolyl, such as indole-2-yl, -3-yl or -5-yl, indolinyl, such as indolin-2-yl, benzimid¬ azolyl, such as 5-benzimidazolyl, quinolinyl, such as quinoline-8-yl, -6-yl, -4-yl, -3-yl or -2-yl, isoquinolyl, such as isoquinoline-1-yl, benzofuranyl, isobenzofuranyl, 2,3-dihydrobenzo-fu- ranyl, such as 2,3-dihydrobenzofuran-5-yl, chromanyl, cyclohexa[b]pyrrolyl, cyclohexa[b]py- ridyl, cyclohexa[b]pyrazinyl, cyclohexa[b]pyrimidinyl, pyrrolidinyl, pyrrolinyl, imidazolidyl, piperidyl, piperazinyl, morpholinyl, thiomorpholinyl, S,S-dioxo-thiomorpholinyl, 4,5,6,7- tetrahydroindolyl, 1 ,2,3,4-tetrahydroquinolyl or 1 ,2,3,4-tetrahydroisoquinolyl, or (altematively or in addition to the group of moieties mentioned so far) chromenyl (= 1 H- or 2H-benzo- pyranyl), such as 2H-chromen-3-yl; with heterocyclyl, for example one of the last-mentioned radicals, being unsubstituted or substituted by one or more, preferably one or two, substituents independently selected from lower alkyl, for example methyl, phenyl, 1- or 2- naphthyl, phenyl-lower alkyl, for example benzyl, hydroxy-lower alkyl, for example hydro¬ xymethyl or 2-hydroxyethyl, hydroxy, lower alkoxy, for example methoxy or ethoxy, amino, lower alkylamino, for example methyl-, ethyl- or tert-butyl-amino, di-lower alkylamino, for example dimethyl- or diethyl-amino, carboxy, lower alkoxycarbonyl, for example methoxy-, isopropoxy-, sec-butoxy- or tert-butoxy-carbonyl, phenyl- or naphthyl-lower alkoxycarbonyl, for example benzyloxycarbonyl, halogen, for example fluorine, chlorine, bromine or iodine, especially chlorine or bromine, lower alkanoyl, for example acetyl or pivaloyi, nitro, oxo and cyano; more preferably heterocyclyl being selected from imidazolyl, such as imidazole-4-yl, thiazolyl, such as 4- or 5-thiazolyl, pyridyl, such as pyridin-3- or pyridin-4-yl, pyrazinyl, such as pyrazin-2-yl, indolyl, such as indole-2-yl, -3-yl or -5-yl, indolinyl, such as indolin-2-yl, benzimidazolyl, such as 5-benzimidazolyl, quinolinyl, such as quinoline-8-yl, -6-yl, -4-yl, -3-yl or -2-yl, isoquinolyl, such as isoquinoline-1-yl, and 2,3-dihydrobenzofuranyl, such as 2,3- dihydrobenzofuran-5-yl, or (altematively or in addition to the group of moieties mentioned just before) chromenyl (=1 H- or2H-benzopyranyl), such as 2H-chromen-3-yl, these radicals being unsubstituted or substituted as above; most preferably from imidazolyl, such as imidazole-4-yl, thiazolyl, such as 4- or 5-thiazolyl, pyridyl, such as pyridin-3- or pyridin-4-yl, pyrazinyl, such as pyrazin-2-yl, indolyl, such as indole-2-yl, -3-yl or -5-yi, indolinyl, such as indolin-2-yl, benzimidazolyl, such as 5-benzimidazolyl, quinolinyl, such as quinoline-8-yl, -6- yl, -4-yl, -3-yl or -2-yl, isoquinolyl, such as isoquinoline-1-yl, and 2,3-dihydrobenzofuranyi, such as 2,3-dihydrobenzofuran-5-yl, each of which is unsubstituted or substituted by lower alkyl, such as methyl, or amino, or (alternatively or in addition to the group of moieties mentioned just before) chromenyl, such as 2H-chromen-3-yl, that is unsubstituted by 1 to 3 substitutents selected from oxo and hydroxy, especially 7,8-dihydroxy-2-oxo-2H- (benzopyran)-3-yl. In aryl-lower alkylcarbonyl, aryl-lower alkylsulfonyl, heterocyclyl-lower alkylcarbonyl and heterocyclyl-lower alkylsulfonyl with the proviso that in any of the lower alkyl radicals men¬ tioned a methylene group may be replaced with aza, thia or (preferably) oxa, preferably the oxa being bound to the respective aryl or heterocylyl or to the carbonyl group in formula I, the lower alkyl or the lower alkyl wherein a methylene group may be replaced with oxa, aza or thia can be linear or branched and is preferably selected from methyl (forming methyle¬ ne), 1 , 2-ethyl (forming 1 ,2-ethylene), 1 , 1 -ethyl (forming methyl-methylene), methoxy whe¬ rein the methyl is bound to the aryl or heterocyclyl and the oxygen is bound to the carboxy group or the methyl is bound to the carbonyl and the oxygen is bound to the aryl or hete¬ rocyclyl group (forming 1 -oxaethylene = -CH 2 -O-; or 2-oxaethylene = -O-CH 2 -), 1 ,3-propyl (forming a 1 ,3-propylene = -CH 2 -CH 2 -CH 2 -), ethoxy wherein the terminal methylene is bound to the aryl or heterocyclyl and the oxygen is bound to the carbonyl group or ethoxy wherein the terminal methylene is bound to the carbonyl and the oxygen is bound to the aryl or hete¬ rocylyl (forming 1 -oxa-3-propylene = -CH 2 -CH 2 -O- or 3-oxa-1 -propylene = -O-CH 2 -CH 2 -). The radicals given in parenthesiws are to be regarded in the following way: The bond on the left of each radical is to be regarded to be directed to the N-terminus in formula I, the bond on the right is to be regarded to be directed to the C-terminus of formula I. In arylcarbonyl X, the aryl moiety is preferably defined as above; more preferably, arylcar¬ bonyl is selected from benzoyi or naphthoyl and, even more preferably, from benzoyi sub¬ stituted with amino; lower alkylamino; amino-lower alkyl; hydroxy; lower alkoxy; amino and hydroxy; amino and lower alkoxy; carboxy; lower-alkoxycarbonyl; cyano; halogen, especially chloro; lower-alkylthio; or lower alkylsulfinyl; or (altematively or in addition to the group of moieties mentioned just before) selected from naphthoyl or hydroxy-naphthoyl, such as naphthalene-2-yl-carbonyl or 6-hydroxy-naphthalene-2-yl-carbonyl, and, less preferably, from fluorenylcarbonyl, such as fluoren-9-ylcarbonyl; especially from 4-aminobenzoyl, 3- aminobenzoyl, 2-aminobenzoyl, 4-lower alkylamino-benzoyl, such as 4-methylamino- benzoyl, 4-(amino-lower alkyl)-benzoyl, such as 4-(methylamino)-benzoyl, 4-hydroxy- benzoyl, 4-lower alkoxy-, such as 4-methoxybenzoyl, 4-amino-2-hydroxy-benzoyl, 4-amino- 3-lower alkoxy-benzoyl, such as 4-amino-3-methoxy-benzoyl, 4-carboxybenzoyl, 4-lower alkoxycarbonyl-benzoyl, such as 4-methoxycarbonyl-benzoyl, 4-cyanobenzoyl, 4-lower alkylthio-benzoyl, such as 4-methylthiobenzoyl, and 4-lower alkylsulfinyl-benzoyl, such as 4- lower methylsulfinyl-benzoyl, or (alternatively or in addition to the group of moieties mentioned just before) from naphthalene-2-yl-carbonyl or 6-hydroxy-naphthelene-2-yl- carbonyl; and most preferably from 3- or especially 4-aminobenzoyl, or (alternatively or in addition to the group of moieties mentioned just before) 6-hydroxy-naphthalen-2-yl- carbonyl. In cycloalkylcarbonyl X, cycloalkyl is preferably as defined above; more preferably, cyclo¬ alkylcarbonyl is C3-C7-, especially C - C 5 - or C 6 -cycloalkylcarbonyl, such as cyclohexyl-car- bonyl, and is unsubstituted or substituted by amino or anneiated to a benzo ring; most pre¬ ferably cyclohexylcarbonyl, 1 ,2,3,4-tetrahydronaphthylcarbonyl, such as 1 ,2,3,4-tetrahydro- naphthyl-2-carbonyl, or especially 1 -amino-cyclohexylcarbonyl or 1-amino-cyclopentylcarbo- nyl. Cyclohexylcarbonyl and especially 1 ,2,3,4-tetrahydronaphthyl-2-carbonyl are most pre¬ ferred. In Tricycloalkylcarbonyl, tricycloalkyl preferably has 8 to 16 carbon atoms and is, for ex¬ ample, tricyclo[5.2.1.0 2,6 ]dec-8-yl or especially adamantyl, preferably 1 -adamantyl. 1- Adamantylcarbonyl is especially preferred. In arylsulfonyl X [= aryl-(SO 2 )-] , the aryl moiety is preferably defined as above; more pre¬ ferably, arylsulfonyl is 2-or 3-napthylsulfonyl which is substituted with amino or mono- or di- lower alkylamino, such as dimethylamino, especially 5-dimethylamino-naphthalenesulfonyl. In heterocyclylcarbonyl, the heterocyclyl moiety is preferably as defined above; more pre¬ ferably, heterocyclylcarbonyl is selected from pyridylcarbonyl which is unsubstituted or sub¬ stituted with amino, such as pyridin-4-yl- or pyridin-3-ylcarbonyl, or amino-pyridin-3-yl-car- bonyl, such as 2- or 6-amino-pyridin-3-ylcarbonyl, benzimidazolylcarbonyl, such as benz- imidazol-5-ylcarbonyl, quinolinyl-carbonyl, such as quinoline-2-, quinoline-3- or quinoline-6- ylcarbonyl, 2,3-dihydrobenzofuranylcarbonyl, such as 2,3-dihydrobenzofuran-5-ylcarbonyl, and indolylcarbonyl, such as indole-5-yl-, indole-3-yl- or indole-2-yl-carbonyl, or (alternatively or in addition to the group of moieties mentioned just before) chromenyl, such as 2H- chromen-3-yl, that is unsubstituted by 1 to 3 substitutents selected from oxo and hydroxy, especially 7,8-dihydroxy-2-oxo-2H-(benzopyran)-3-yl; most preferably from quinoline-6-yl- carbonyl and especially from indolylcarbonyl, such as indole-3- and indole-5-ylcarbonyl, or (alternatively or in addition to the group of moieties mentioned just before) 7,8-dihydroxy-2- oxo-2H- (benzopyran) -3-yl. In heterocyclylsulfonyl X [= heterocyclyl- (SO 2 )-]; the heterocyclyl moiety is preferably as defined above; more preferably, heterocyclylsulfonyl is selected from quinolinylsulfonyl, such as quinoline-8-ylsulfonyl. In carbamoyl-lower alkanoyl, lower alkanoyl is especially propionyl. Preferred is 3- carbamoylpropionyl. In aryl-lower alkylcarbonyl X, with the proviso that in the lower alkyl radical mentioned a methylene group may be replaced with oxa, aza or thia (the latter two being less preferred than oxa), the aryl moiety is preferably as defined above for aryl (most preferably lower alkylaminophenyl, such as 2-, 3- or 4-acetylaminophenyl, or especially hydroxyphenyl, such as 3-hydroxyphenyl, or (in the sequence of growing preference) 2-amino-, 3,5-diamino-, 4- amino- or 3-aminophenyl); or (alternatively or in addition to the group of moieties mentioned just before) amino-lower alkylphenyl, such as aminomethyl-phenyl, or preferably 3,4- dihydroxyphenyl; and the lower alkyl or the lower alkyl wherein a methylene group may be replaced with oxa, aza or thia can be linear or branched and is preferably selected from methyl (forming methylene), 1 , 2-ethyl (forming 1 , 2-ethyl ene), 1 ,1 -ethyl (forming methyl- methylene), methoxy wherein the methyl is bound to the aryl and the oxygen is bound to the carboxy group or the methyl is bound to the carbonyl and the oxygen is bound to the aryl group (forming 1 -oxaethylene = -CH 2 -O-; or 2-oxaethylene = -O-CH 2 -), 1 ,3-propyl (forming a 1 ,3-propylene = -CH 2 -CH 2 -CH 2 -), ethoxy wherein the terminal methylene is bound to the aryl and the oxygen is bound to the carbonyl group or ethoxy wherein the terminal methylene is bound to the carbonyl and the oxygen is bound to the aryl (forming 1 -oxa-3-propylene = - CH 2 -CH 2 -O- or 3-oxa-1 -propylene = -O-CH 2 -CH 2 -); more preferred is a moiety selected from phenyl-methoxycarbonyl wherein the phenyl residue is unsubstituted or substituted with amino in the (in growing preference) 2-, 3- and 5-, 4- or 3-position of the phenyl ring; (±)-, (+) or (-)-1-(3-aminophenyl)ethyloxycarbonyl; hydroxybenzyloxy- or hydroxyphenyl-2-etho- xycarbonyl, such as 3-hydroxybenzyloxycarbonyl or 3-hydroxyphenyl-2-ethoxycarbonyl; (with less preference) lower alkanoylamino-phenyloxymethylcarbonyl, such as 2-, 3- or especially 4-acetylaminophenyloxymethylcarbonyl, aminophenyloxymethylcarbonyl, such as 3- or 4-aminophenyloxymethylcarbonyl; aminophenyl-lower alkylcarbonyl, such as 4-ami- nophenyl-acetyl or 3-(3-aminophenyl)-propionyl; and (with still less preference) benzyloxy¬ carbonyl or phenylacetyl. More preferred is also (alternatively or in addition to the group of moieties mentioned just before) 3-(3,4-dihydroxyphenyl)-propionyi or 2-(3,4-dihydroxy- phenyl)-acetyl. In cycloalkyl-lower alkylcarbonyl X, cycloalkyl is preferably as defined above; more prefer¬ ably, cycloalkyl-lower alkylcarbonyl is C 3 -C 7 -, especially C 4 - C 5 - or C 6 -cycloalkyl-d-C -car- bonyl, such as 3-cyclohexylpropanoyl, and is unsubstituted or substituted by amino; most preferably 1 -amino-cyclohexylcarbonyl or 1-amino-cyclopentylcarbonyl; or (alternatively or in addition to the group of moieties mentioned just before) 3-(cyclohexyl)-propionyl. In aryl-lower alkylsulfonyl X, with the proviso that in the lower alkyl radical mentioned a methylene group may be replaced with oxa, aza or thia; aryl and the lower alkyl or lower alkyl wherein a methylene group is replaced with oxa, aza or thia are preferably as described above. In heterocyclyl-lower alkylcarbonyl X, with the proviso that in the lower alkyl radical mentio¬ ned a methylene group may be replaced with oxa, aza or thia; the heterocyclyl moiety is preferably as defined above, more preferably being selected from unsubstituted or amino- or lower alkyl-substituted thiazolyl, such as 4-methyl-thiazol-5-yl or 2-amino-thiazole-4-yl, indolyl, such as indole-3-yl, and benzimidazolyl, such as benzimidazol-5-yl; and the lower alkyl or the lower alkyl wherein a methylene group may be replaced with oxa, aza or thia can be linear or branched and is preferably selected from methyl (forming methylene), 1 ,2- ethyl (forming 1 ,2-ethylene), 1 , 1 -ethyl (forming methyl-methylene), methoxy wherein the methyl is bound to the heterocyclyl and the oxygen is bound to the carboxy group or the methyl is bound to the carbonyl and the oxygen is bound to the heterocyclyl group (forming 1 -oxaethylene = -CH 2 -O-; or 2-oxaethylene = -O-CH 2 -), 1 ,3-propyl (forming a 1 ,3-propylene = -CH 2 -CH 2 -CH 2 -), ethoxy wherein the terminal methylene is bound to the heterocyclyl and the oxygen is bound to the carbonyl group or ethoxy wherein the terminal methylene is bound to the carbonyl and the oxygen is bound to the heterocylyl (forming 1 -oxa-3-propyle- ne = -CH 2 -CH 2 -O- or 3-oxa-1 -propylene = -O-CH 2 -CH 2 -). More preferred is unsubstituted or lower alkyl-substituted 2-(thiazolyl)-ethoxycarbonyl, such as 2-(4-methyl-thiazol-5-yl)-ethoxy- carbonyl, unsubstituted or amino-substituted thiazolyl-lower alkylcarbonyl, such as 2-amino- thiazole-5-ylacetyl, or especially indolyl-lower alkylcarbonyl, such as indole-3-yl-acetyl, 3- (indole-3-yl)propionyl or 4-(indole-3-yl)butyroyl. ln heterocyclyl-lower alkylsulfonyl with the proviso that in the lower alkyl radical mentioned a methylene group may be replaced with oxa, aza or thia, the heterocyclyl moiety and the lower alkyl or the lower alkyl radical wherein a methylene group is replaced with oxa, aza or thia are preferably as defined above, respectively. In aryl-lower alkenylcarbonyl X, aryl is preferably as defined above, especially being selec¬ ted from phenyl which is substituted by 1 to 2 moieties independently selected from lower alkoxy, preferably methoxy, and especially hydroxy, while the lower alkenyl radical prefer¬ ably is linear and has one double bond and 2 to 7 carbon atoms, preferably being a 1 ,2- vinyl radical. Preferred is cinnamoyl substituted by 1 to 2 moieties selected independently from methoxy and especially hydroxy, especially p-hydroxycinnamoyl (= 4-hydroxycinna- moyl), m-hydroxy-p-methoxy-cinnamoyl (= 3-hydroxy-4-methoxycinnamoyl) or preferably m,p-dihydroxy-cinnamoyl (= 3,4-dihydroxycinnamoyl). In heterocyclyl-lower alkenylcarbonyl X, the heterocyclyl moiety is preferably as defined above, especially being selected from imidazolyl, such as 4-imidazolyl, and from indolyl, such as indole-3-yl, while the lower alkenyl radical preferably is linear and has one double bond and 2 to 7 carbon atoms, preferably being a 1 ,2-vinyl radical; more preferably, hete¬ rocyclyl-lower alkenylcarbonyl is selected from imidazolyl-lower alkenylcarbonyl, such as imidazole-4-yl-lower alkenylcarbonyl, especially imidazole-4-yl-acryloyl, and indolyl-lower alkenylcarbonyl, such as indole-3-ylacryloyl. For X, arylcarbonyl; heterocyclylcarbonyl; aryl-lower alkylcarbonyl, heterocyclyl-lower alkylcarbonyl with the proviso that in the lower alkyl radical mentioned a methylene group may be replaced with oxa, aza or thia (the latter two being lesss preferred than oxa); and heterocyclyl-lower alkenylcarbonyl are especially preferred, the respective substituents being marked as preferred in the definitions given above being more preferred. In addition or alternatively to this group of moieties, carbamoyl-lower alkanoyl, cycloalkyl-carbonyl and aryl-lower alkylcarbonyl are especially preferred. Lower alkanoyl X, which may be present only if Y is a secondary or tertiary amino group, is especially acetyl, but may also be pivaloyi. - 16 Halo-lower alkanoyl preferably has one to three halogen substituents, preferably selected from chloro and fluoro, and is for example trifluoroacetyl or trichloroacetyl. Lower-alkoxycarbonyl X, which may be present only if Y is a secondary or tertiary amino group, is especially methoxycarbonyl, ethoxycarbonyl or tert-butoxycarbonyl. Aryl-lower alkoxycarbonyl X, which may be present only if Y is a secondary or tertiary amino group, has an aryl moiety as defined above, especially phenyl or fluorenyl, and is especially benzyloxycarbonyl or fluoren-9-ylmethoxycarbonyl. Cycloalkyl-lower alkoxycarbonyl X, which may be present only if Y is a secondary or tertiary amino group, has a cycloalkyl moiety as defined above and is especially cyclohexyl-lower alkoxycyrbonyl, such as cyclohexylmethyl-oxycarbonyl. PTI is the bivalent radical of tyrosine (-Tyr-) or preferably a bivalent radical of phosphotyrosine or a phosphotyrosine mimic. A bivalent radical of phosphotyrosine is especially (D,L), (D)- or preferably (L)-4-(O- Phosphono)-Tyr [= (O-PO 3 H 2 )Tyr] (bound N-terminally via the imino group resulting from the α-amino group and C-terminally via the carbonyl group resulting from its α-carboxy group), preferably the radical of the formula A A bivalent radical of a phosphotyrosine mimic PTI is defined as any radical that is able to replace a phosphotyrosine radical which resembles, but is structurally different from the respective phosphotyrosine radical and which cannot lose its phosphono-group too easily due to hydrolysis. Preferably, such a mimic is selected from the respective bivalent radical (which is bound N-terminally via the imino group resulting from the α-amino group and C- terminally via the carbonyl group resulting from its α-carboxy group) of an amino acid selec¬ ted from phosphonomethyl-phenylalanine, especially 4-phosphonomethyl-phenylalanine, phosphono-(α-fluoro)methyl-phenylalanine, especially 4-phosphono-(α-fluoro)methyl-phe- nylalanine, phosphono-(α,α-difluoro)methyl-phenylalanine, especially 4-phosphono-(α,α- difluoro)methyl-phenylalanine, phosphono-(α-hydroxy)methyl-phenylalanine, especially 4- phosphono-(α-hydroxy)methyl-phenylalanine, O-sulfo-tyrosine, such as 4-(O-sulfo)tyrosine, dicarboxymethoxy-phenylalanine (= (HOOC) 2 -CH 2 -O-phenylalanine), especially p- (dicarboxymethoxy)-phenylalanine; (less preferably) phosphonophenylalanine, such as 4- phosphonophenylalanine; aspartic acid, glutamic acid, phosphoserine and phosphothreonine, each of which is present in the (D,L)-, D- or preferably the L-form. For PTI, a bivalent radical of phosphotyrosine and especially a bivalent radical of phos- phono-(α,α-difluoro)methyl-phenylalanine, especially 4-phosphono-(α,α-difluoro)methyl- phenylalanine, or a bivalent radical of phosphonomethyl-phenylalanine, especially 4- (phosphonomethyl)-phenylalanine, is most preferred. AA stands for a natural or unnatural amino acid, and is preferably a bivalent radical of an α- or β-amino acid which is preferably bonded N-terminally by way of its α- or β-amino group and C-terminally by way of its carboxy group and is preferably selected from the group comprising a bivalent radical of a natural α- amino acid having the L-configuration, such as those normally occurring in proteins, or an epimer of such an amino acid, that is to say having the unnatural D-configuration, or a (D,L)-isomeric mixture thereof; or a homologue of such an amino acid, for example a β-amino acid or an α-amino acid wherein the amino acid side chain has been shortened by one or two methylene groups or lengthened to up to 10 carbon atoms, such as an α-amino alkanoic acid with 5 up to and including 10 carbon atoms in a linear chain, an unsubstituted or substituted aromatic (α-aryl or α-aryl lower alkyl) amino acid wherein the aryl radical has from 6 to 14 carbon atoms, for example a homophenylalanine or a substituted phenylalanine or phenylglycine wherein the phenyl may be mono- or poly-substituted by lower alkyl, for example methyl, lower alkoxy, for example methoxy, lower alkanoyloxy, for example acetoxy, amino, lower alkylamino, for example methylamino, di-lower alkylamino, for example dimethylamino, lower alkanoylamino, for example acetylamino or pivaloylamino, lower alkoxycarbonylamino, for example tert-butoxy- carbonylamino, arylmethoxycarbonylamino wherein aryl preferably has from 6 to 14 carbon atoms, for example benzyloxycarbonylamino or 9-fiuorenylmethoxycarbonylamino, halogen, for example fluorine, chlorine, bromine or iodine, carboxy and/or by nitro, a benzo-fused phenylalanine or phenylglycine, such as α-naphthylalanine, and a hydrogenated phenyl¬ alanine or phenylglycine, such as cyclohexylalanine or cyclohexylglycine, or an α-amino heterocyclyl-lower alkanoic acid wherein heterocyclyl preferably is a single or double ring system having from 3 to 10 ring atoms, is bonded via a carbon atom or via a nitrogen atom and. contains up to 3 further hetero atoms selected from oxygen, nitrogen, sulfur, and sulfur linked to 1 or 2 oxygen atoms, and may be unsaturated or partially or fully saturated, for example furyl, pyrrolyl, pyrrolidinyl, morpholinyl, pyridyl or indolyl, a cyclic α-amino-(α,α- lower alkylene)-carbonic acid; or an α-amino-[(C 6 -C 8 )-bicyclo]-carbonic acid; each being present in the L-, D- or (D,L)-configuration and in unprotected or amino-, carboxy- or sulfhydryl-protected form. Especially preferred is the bivalent radical, bonded via its α-amino and its α- or β-carbonyl group, of an amino acid selected from glycine (H-Gly-OH), alanine (H-Ala-OH), β-alanine (H- βAla-OH), valine (H-Val-OH), norvaline (α-aminovaleric acid), leucine (H-Leu-OH), iso¬ leucine (H-lle-OH), norleucine (α-aminohexanoic acid, H-Nle-OH), α-amino-n-decanoic acid, serine (H-Ser-OH), homoserine (α-amino-γ-hydroxybutyric acid), threonine (H-Thr-OH), methionine (H-Met-OH), cysteine (H-Cys-OH), S-acetylaminomethyl-cysteine (H-Cys(Acm)- OH), proline (H-Pro-OH), trans-3- and trans-4-hydroxyproline, phenylalanine (H-Phe-OH), tyrosine (H-Tyr-OH), 4-aminophenyialanine, 4-nitrophenylalanine, 4-chlorophenylalanine, 4- carboxyphenylalanine, β-phenylserine (β-hydroxyphenylalanine), phenylglycine, α- naphthylalanine (H-Nal-OH), cyclohexylalanine (H-Cha-OH), cyclohexylglycine, tryptophan (H-Trp-OH), indoline-2-carboxylic acid, 1 ,2,3,4-tetrahydroisoquinoline-3-carboxylic acid, aspartic acid (H-Asp-OH), asparagine (H-Asn-OH), aminomalonic acid, aminomalonic acid monoamide, glutamic acid (H-Glu-OH), glutamine (H-Gln-OH), histidine (H-His-OH), arginine (H-Arg-OH), lysine (H-Lys-OH), N'-benzyl-N'-methyl-lysine, N ε ,N e -dibenzyl-lysine, δ-hydroxy- lysine, ornithine (α,δ-diaminovaleric acid), α-amino-cyclopentane carboxylic acid (H-Ac 5 c- OH), α-amino-cyclohexane carboxylic acid (H-Ac 6 c-OH), α-amino cycloheptane carboxylic acid (H-Ac 7 c-OH), α-(2-amino-2-norbornane)-carboxylic acid (H-Nbo-OH), α,γ- diaminobutyric acid and α,β-diaminopropionic acid; or (alternatively or in addition to the group of moieties mentioned just before) homophenylalanine (H-Hph-OH = 2-amino-4- phenyl-butyric acid) and α-tert-butylglycine (H-Tle-OH = tert-leucine); it being possible for each of the mentioned amino acids (with the exception of glycine or any other amino acid without asymmetric carbon atom) to be in the D-, L- or (D,L)-form, preferably in the L- or in the D-form. H-DHph-OH is D-homophenylalanine. More preferably, the bivalent radical -(AA) n - in formula I is an analogue of an SH2 domain binding site of a protein with phosphotyrosine of a mammal, especially a human, for example one of the binding sites mentioned in Songyang et al., Cell 72, 767-778 (1993), e.g. (i) in the case of the Src family SH2 binding proteins, especially an analogue of the human CD3 ζ chain following Tyr 110 (that is, -Asn-Glu-Leu-Gln-Lys-Asp-Arg-Met-Ala-Glu- Ala-) or Tyr 122 (that is, -Ser-Glu-lle-Gly-Met-), an analogue of the human Rb-associated rb 1 10 chain following Tyr 321 (that is, -Glu-Glu-lle-Tyr-Leu-), an analogue of the human vav oncogene chain following Tyr 126 (that is, -Glu-Asp-Leu-Met-Arg-), an analogue of the human ErbB3 chain following Tyr 1270 (that is, -Glu-Glu-Met-Arg-Ala-), an analogue of the human T cell CD7 chain following Tyr 222 (that is, -Glu-Asp-Met-Ser-His-) or an analogue of the human G2 cyclin b chain following Tyr 255 (that is, -Glu-Asp-Met-Ser-His-), (ii) in the case of the Abl SH2 binding proteins, especially an analogue of the human B cell CD19 chain following Tyr 409 (that is, -Glu-Glu-Pro-Asp-Ser-) or Tyr 439 (that is, -Glu-Asn-Pro- Glu-Asp-), an analogue of the human B cell CD 72 chain following Tyr 39 (that is, -Glu-Asn- Val-Gln-Val-), an analogue of the human colony-stimulating factor 1 receptor chain following Tyr 923 (that is, -Thr-Asn-Leu-Pro-Ser-), an analogue of the human JunB chain following Tyr 182 (that is, -Thr-Asn-Leu-Ser-Ser-), an analogue of the human protein kinase C β-1 chain following Tyr 662 (that is, -Thr-Asn-Pro-Glu-Phe-), (iii) in the case of Crk SH2 binding proteins, especially an analogue of the human Fer tyrosine kinase chain following Tyr 615 (that is, -Asp-His-Pro-Asn-lle-), (iv) in the case of Nek SH2 binding proteins, especially an analogue of the human cel! cylce gene 1 protein chain following Tyr 139 (that is, -Asp-Glu- Asp-Asp-Tyr-), (v) in the case of Sem-5/Grb2 SH2 binding proteins, especially an analogue of the human EGF receptor chain following Tyr 1092 (that is, -lle-Asn-Gln-Ser-Val-), an analogue of the human EGF receptor chain following Tyr 1138 (that is, -Leu-Asn-Thr-Val- Gln-), an analogue of the human SHC chain following Tyr 317 (that is, -Val-Asn-Val-Gln- Asn, an analogue of the human HGF receptor chain following Tyr 1374 (that is, -Val-Asn- Val-Leu-Cys-), an analogue of the human ErbB2 chain following Tyr 1139 (that is, -Val-Asn- Gln-Pro-Asp-), an analogue of the human ErbB3 chain following Tyr 1200 (that is, -Met-Asn- Arg-Arg-Arg-) or Tyr 1262 (that is, -Met-Asn-Arg-Gln-Arg-), an analogue of the human IGF-1 receptor chain following Tyr 1125 (that is, -Leu-Asn-Ala-Asn-Lys-), an analogue of the human Fit tyrosine kinase chain following Tyr 1213 (that is, -Val-Asn-Ala-Phe-Lys-), an analogue of the human insulin receptor chain following Tyr 1149 (that is, -Leu-Asn-Ala-Lys- Lys-), an ana-logue of the human CD45 PTPase chain following Tyr 706 (that is, -lle-Asn- Ala-Ser-Tyr-), or Tyr 1015 (that is, -lle-Asn-Ala-Ser-Phe-), (vi) in the case of p85 N-terminal SH2, especially an analogue of the human PDGF receptor β chain following Tyr 740 (that is, -Met-Asp-Met-Ser-Lys-Asp-Glu-Ser-Val-Asp-) or Tyr 751 (that is, -Val-Pro-Met-Leu-Asp-), an analogue of the human c-Kit chain following Tyr 721 (that is, -Met-Asp-Met-Lys-Pro-), an analogue of the human ErbB3 chain following Tyr 1257 (that is, -Ala-Ala-Met-Gly-Ala-Cys- Pro-Ala-Ser-Glu-Gln-Gly-), Tyr 1270 (that is, -Glu-Glu-Met-Arg-Ala-), Tyr 1241 (that is, -Glu- Met-Asn-Arg-GIn-), Tyr 1257 (that is, -Ala-Ala-Met-Gly-Ala-), Tyr 922 (that is, -Met-Val-Met- Val-Lys-), Tyr 1035 (that is, -Met-Pro-Met-Asn-GIn-), Tyr 1 ,178 (that is, -Glu-Tyr-Met-Asn- Arg-), or Tyr 1203 (-Glu-Tyr-Met-Asp-Val-), (vii) in the case of p85 C-terminal SH2, especially the same sites as for p85 N-terminal SH2, (vii) in the case of PLC-γ C-terminal SH2, especially an analogue of the human PDGF receptor β chain following Tyr 1021 (that is, -lle-lle-Pro-Leu-Pro-), an analogue of the human PDGF receptor α chain following Tyr 1018 (that is, -lle-lle-Pro-Leu-Pro-), an analogue of the human ErbB2 chain following Tyr 1127 (that is, -Val-Ala-Pro-Leu-Thr-), (viii) in the case of PLC-γ N-terminal SH2 binding proteins, especially an analogue of the human basic FGF receptor I, II, II, IV chain following <=Tyr 766 (that is, -Leu-Asp-Leu-X-X-), an analogue of the human EGF receptor chain following Tyr 978 (that is, -Leu-Val-lle-Gln-Gly-) or Tyr 1197 (that is, -Leu-Arg-Val-Ala-Pro-), an analogue of the human ErbB2 chain following Tyr 1248 (that is, -Leu-Gly-Leu-Asp-Val-), and (ix) in the case of SHPTP2 N-terminal SH2 binding proteins, especially an analogue of the human PDGF receptor β chain following Tyr 1009 (that is, -Thr-Ala-Val-Gln-Pro-) or Tyr 1021 (that is, -lle-lle-Pro-Leu-Pro-), an analogue of the human PDGF receptor α chain following Tyr 1018 (that is, -lle-lle-Pro-Leu-Pro-), Tyr 988 (that is, -lle-Gly-Val-Thr-Tyr-) or Tyr 720 (that is, -Val-lle-Leu-Ser-Phe-), an analogue of the human ErbB3 chain following Tyr 1159 (that is, -Val-Met-Pro-Asp-Thr-) or Tyr 471 (that is, -Val-lle-Val-Glu-Tyr-), an analogue of the human Fit receptor type tyrosine kinase chain following Tyr 1169 (that is, - lle-Pro-lle-Asn-Ala-), an analogue of the human Kit receptor type tyrosine kinase chain following Tyr 568 (that is, -Val-Tyr-lle-Asp-Pro-), an analogue of the human Ros receptor type tyrosine kinase chain following Tyr 234 (that is, -lle-lle-Leu-Glu-Leu-), an analogue of the human HGF receptor (Met) chain following Tyr 1367 (that is, -Val-His-Val-Asn-Ala-) or Tyr 1374 (that is, -Val-Asn-Val-Leu-Cys-); and (x) most especially an analogue of the Epidermal Growth Factor Receptor (EGFR) sequence following Tyr 1068, the binding site for Grb2 SH2 (see Buday et al., Cell 73, 611- 620 (1993)), that is the sequence lle-Asn-Gln-Ser-Val-Pro-Lys-Arg Pro-Aia-Gly-Ser-Val-Gln- Asn, preferably -lle-Asn-Gln-Ser-; wherein in each case one or more amino acids are replaced by analogues which still allow for binding to the respective SH2-comprising protein, especially Grb2, or 1 or more amino acids are deleted, preferably 1 or more amino acids of the sequence -lle-Asn-Gln-Ser-, more preferably 1 , 2 or up to 3 amino acids of the sequence -lle-Asn-GIn- being deleted. Preferably, the -Asn- in position 2 of the mentioned sequence following Tyr 1068 in EGFR is present as such, while the amino acids in the other positions may be replaced with one of the other amino acids mentioned above or (as far as the C-terminal amio acid(s) following the Asn are concemed) may be deleted. More preferably, -(AA) n - has one of the following meanings: • A bivalent radical of a tripeptide of the formula -(AA 1 )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is preferably selected from -lie-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly- and -Phe- or (alternatively or in addition to the group of moieties mentioned just before) from -Ac^-, -Nbo-, -Met-, -Pro-, -βAla-, -Gin-, -Glu-, -DHph-, -HPh- and -tLe-, most preferably -He-, -Ac 5 c-, -Ac 6 c-, -Asp- or -Gly- or (alternatively or in addition to the group of moieties mentioned just before) - Ac 7 c-, -Nbo- and -Gin-; -(AA 2 )- is preferably selected from -Asn-, and also from -βAla- and -Gly-, or (altematively or in addition to the group of moieties mentioned just before), from -lie-, -βAla- and Gin; most preferably -Asn-; and -(AA 3 )- is preferably selected from -Val-, and -β-Ala, and also from -Gly-, -Gin-, -Val-, -Asp- and -Ac 5 c- ; or, less preferably, • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- and -(AA 2 )- preferably have the meanings given above, preferably -(AA 1 )- being -lie- or -Ac 6 c-, or (altematively or in addition to the group of moieties mentioned just before) -ACyC-, -Nbo- and -Gin-; and -(AA 2 )- being -Asn- (preferred) or also -βAla-; • or (even less preferably) simply a bivalent radical of an amino acid selected from the amino acids mentioned above, especially -Ile- or (altematively or in addition to the group of moieties mentioned just before) -Ac 6 c-, -Nbo- and Ac 5 c-. A C-terminal protecting group Y is preferably an esterifying group, thus leading to an esterified C-terminal carboxy group. More preferred is a lower alkoxy group that is preferably branched in the 1 -position of the lower alkoxy group or substituted in the 1 - or 2- position of the lower alkoxy group by (one) suitable substituent(s). A lower alkoxy group that is branched in the 1 -position of the lower alkoxy group is, for example, tert-lower alkoxy, for example tert-butoxy. A lower alkoxy group that is substituted in the 1 - or 2-position of the lower alkoxy group by (one) suitable substituent(s) is, for example, arylmethoxy having one or two aryl radicals, wherein aryl is preferably phenyl that is unsubstituted or mono-, di- or tri-substituted, for example, by lower alkyl, for example tert-lower alkyl, such as tert-butyl, lower alkoxy, for example methoxy, hydroxy, halogen, for example chlorine, and/or by nitro, for example benzyloxy, benzyloxy substituted by the mentioned substituents, for example 4-nitro- benzyloxy or 4-methoxybenzyloxy, diphenylmethoxy or diphenylmethoxy substituted by the mentioned substituents, for example di(4-methoxyphenyl)methoxy; 1 -lower alkoxy-iower alkoxy, for example methoxymethoxy, 1 -methoxyethoxy or 1 -ethoxyethoxy, 1 -lower alkyl- thio-lower alkoxy, for example 1 -methylthiomethoxyl or 1 -ethylthioethoxy, aroylmethoxy wherein the aroyl group is preferably benzoyi that is unsubstituted or substituted, for example, by halogen, such as bromine, for example phenacyloxy, 2-halo-lower alkoxy, for example 2,2,2-trichloroethoxy, 2-bromoethoxy or 2-iodoethoxy, as well as 2-(tri-substituted silyl)-lower alkoxy wherein the substituents are each independently of the others selected from lower alkyl, phenyl-lower alkyl, cycloalkyl or phenyl each of which is unsubstituted or substituted as above, for example 2-tri-lower alkylsilyl-lower alkoxy, such as 2-tri-lower alkyl- silylethoxy, for example 2-trimethylsilylethoxy or 2-(di-n-butyl-methyl-silyl)-ethoxy, or tri- phenylsilylethoxy. A C-terminal protecting Y group can furthermore be an organic silyloxy group. An organic silyloxy group is, for example, a tri-lower alkylsilyloxy group, for example trimethylsilyloxy. The silicon atom of the silyloxy group can also be substituted by two lower alkyl groups, for example methyl groups. A C-terminal protecting group Y is preferably tert-lower alkoxy, for example tert-butyloxy, benzyloxy, 4-nitrobenzyloxy, 9-fluoreny I methoxy or diphenylmethoxy. A primary, secondary or tertiary amino group Y is preferably a free amino group, a mono- or disubstituted amino group the substituents of which are preferably selected from the group comprising lower alkyl, such as methyl, ethyl; isobutyl or 3-methylbutyl; octyl, such as 2- ethyl-hexyl; aryloxy-lower alkyl, especially halonaphthyloxy-lower alkyl, such as 2-(1-bromo- naphthalen-2-yloxy)-ethyl, or naphthyloxy-lower alkyl, such as 2-(naphthalen-2-yloxy or naphthalen-1-yloxy)-ethyl; aryl-lower alkyl, such as phenyl-lower alkyl, e.g. benzyl, 3- phenylpropyl, di-phenyl-lower alkyl, such as 2,2-diphenyl-ethyl or 3,3-diphenyl-propyl, (mono- or di-halo-phenyl)-lower alkyl, such as 2-(4-chlorophenyl)ethyl or 3-(2,4- dichlorophenyl)-propyl, naphthalenyl-lower alkyl, such as 3-naphthtalen-1 -ylpropyl or 3- naphthalen-2-ylpropyl, hydroxy-naphthalenyl-lower alkyl, such as 3-(2-hydroxy-naphthalen- 1 -yl)-propyl, or phenanthrenyl-lower alkyl, such as 3-phenanthren-9-yl-propyl; heterocyclyl- lower alkyl, such as pyrrolidinyl-lower alkyl, e.g. 2-(1-pyrrolidinyl)-ethyl, pyridyl-lower alkyl, e.g. 2-(2-pyridyl)-ethyl, furyl-lower alkyl, e.g. 2-furylmethyl, morpholinyl-lower alkyl, e.g. 2-(4- morpholinyl)-ethyl, and indolyl-lower alkyl, e.g. 2-(3-indolyl)-ethyl; cycloalkyl, such as cyclohexyl; and cycloalkyl-lower alkyl, such as cyclohexylmethyl. A disubstituted amino group may also be N-containing heterocyclyl bonded via its nitrogen atom, such as e.g. 1- pyrrolidinyl or 4-morpholinyl. In one preferred aspect of the invention, a primary, secondary or tertiary amino group Y is a free amino group, a mono- or disubstituted amino group the substituents of which are pre¬ ferably selected from the group comprising lower alkyl, e.g. methyl or ethyl, aryl-lower alkyl, such as phenyl-lower alkyl, e.g. benzyl, or heterocyclyl-lower alkyl, such as pyrrolidinyl-lower alkyl, e.g. 2-(1-pyrrolidinyl)-ethyl, pyridyl-lower alkyl, e.g. 2-(2-pyridyl)-ethyl, furyl-lower alkyl, e.g. 2-furylmethyl, morpholinyl-lower alkyl, e.g. 2-(4-morpholinyl)-ethyl, and indolyl-lower alkyl, e.g. 2-(3-indolyl)-ethyl. A disubstituted amino group may also be N-containing hetero¬ cyclyl bonded via its nitrogen atom, such as e.g. 1 -pyrrolidinyl or 4-morpholinyl. Preferably, Y is a primary, secondary or tertiary amino group as defined above, most pre¬ ferably amino (-NH 2 ) or monosubstituted amino selected from lower alkylamino, such as methylamino, ethylamino; isobutylamino or 3-methylbutylamino; octylamino, such as 2-ethyl- hexyl-amino; aryloxy-lower alkylamino, especially halonaphthyloxy-lower alkylamino, such as 2-(1-bromo-naphthalen-2-yloxy)-ethylamino, or naphthyloxy-lower alkylamino, such as 2- (naphthalen-2-yloxy or naphthalen-1 -yloxy)-ethylamino; aryl-lower alkylamino, such as phenyl-lower alkylamino, e.g. benzylamino, 3-phenylpropylamino, di-phenyl-lower alkyl¬ amino, such as 2,2-diphenyl-ethylamino or 3,3-diphenyl-propylamino, (mono- or di-halo- phenyl)-lower alkylamino, such as 2-(4-chlorophenyl)ethylamino or 3-(2,4-dichlorophenyl)- propylamino, naphthalenyl-lower alkylamino, such as 3-naphthtalen-1-ylpropylamino or 3- naphthalen-2-ylpropylamino, hydroxy-naphthalenyl-lower alkylamino, such as 3-(2-hydroxy- naphthalen-1-yl)-propylamino, or phenanthrenyl-lower alkylamino, such as 3-phenanthren- 9-yl-propylamino; cycloalkylamino, such as cyclohexylamino; and cycloalkyl-lower alkylamino, such as cyclohexylmethylamino. Salts of compounds of formula I are especially acid addition salts, salts with bases or, where several salt-forming groups are present, can also be mixed salts or internal salts. Salts are especially pharmaceutically acceptable salts of compounds of formula I. Such salts are formed, for example, from compounds of formula I having an acid group, for example a carboxy group, a sulfo group, or a phosphoryl group substituted by one or two hydroxy groups, and are, for example, salts thereof with suitable bases, such as non-toxic metal salts derived from metals of groups la, Ib, lla and lib of the Periodic Table of the Elements, especially suitable alkali metal salts, for example lithium, sodium or potassium salts, or alkaline earth metal salts, for example magnesium or calcium salts, also zinc salts or ammonium salts, as well as salts formed with organic amines, such as unsubstituted or hydroxy-substituted mono-, di- or tri-alkylamines, especially mono-, di- or tri-lower alkyl¬ amines, or with quaternary ammonium compounds, for example with N-methyl-N-ethyl- amine, diethylamine, triethylamine, mono-, bis- or tris-(2-hydroxy-lower alkyl)amines, such as mono-, bis- or tris-(2-hydroxyethyl)amine, 2-hydroxy-tert-butylamine or tris(hydroxy- methyl) methylamine, N,N-di-lower alkyl-N-(hydroxy-lower alkyl)-amines, such as N,N- dimethyl-N-(2-hydroxyethyl)-amine or tri-(2-hydroxyethyl)-amine, or N-methyl-D-glucamine, or quaternary ammonium salts, such as tetrabutylammonium salts. The compounds of formula I having a basic group, for example an amino group, can form acid addition salts, for example with inorganic acids, for example hydrohalic acids, such as hydrochloric acid, sulfuric acid or phosphoric acid, or with organic carboxylic, sulfonic, sulfo or phospho acids or N-substituted sulfamic acids, for example acetic acid, propionic acid, glycolic acid, succinic acid, maleic acid, hydroxymaleic acid, methylmaleic acid, fumaric acid, malic acid, tartaric acid, gluconic acid, glucaric acid, glucuronic acid, citric acid, benzoic acid, cinnamic acid, mandelic acid, salicylic acid, 4-aminosalicylic acid, 2-phenoxybenzoic acid, 2- acetoxybenzoic acid, embonic acid, nicotinic acid or isonicotinic acid, as well as with amino acids, for example the α-amino acids mentioned hereinbefore, especially glutamic acid and aspartic acid, and with methanesulfonic acid, ethanesulfonic acid, 2-hydroxyethanesulfonic acid, ethane-1 ,2-disulfonic acid, benzenesulfonic acid, 4-methyibenzene-sulfonic acid, naphthalene-2-sulfonic acid, 2- or 3-phosphoglycerate, glucose-6-phosphate, N-cyclohexyl- sulfamic acid (forming cyclamates) or with other acidic organic compounds, such as ascorbic acid. Compounds of formula I having acid and basic groups can also form internal salts. For isolation or purification purposes, it is also possible to use pharmaceutically inaccept- able salts, for example a perchlorate or picolinate salt. The compounds of the invention have useful, in particular pharmacologically useful, proper¬ ties. Surprisingly, it has been found that the compounds of formula I are able to inhibit the interaction between SH2 domains of downstream regulatory proteins, such as Grb2, and phosphoproteins, especially phosphorylated protein tyrosine kinases, such as a phospho¬ protein containing a -Tyr(PO 3 H 2 )-X-Asn- motif, preferably phosphorylated EGFR protein ty¬ rosine kinase (EGFR = Epidermal Growth Factor Receptor) or modified derivatives thereof, but in a broader sense also other phospho-proteins such as SHC or modified derivatives thereof, in a favourable way. They are thus useful in the treatment or prevention of diseases that respond to such inhibition. The ability to inhibit the interaction between the SH2 domain of Grb2 and phosphorylated EGFR can be shown by the following type of assay: The principle of the assay is that a full- length or truncated phosphotyrosine protein immobilized on a solid phase is incubated with a chimeric SH2-GST (GST = glutathione S-transferase) protein or a full length SH2-contai- ning protein-GST fusion protein capable of binding to it, in the presence of a test substance (for review, see Proc. Natl. Acad. Sci. USA 91, 83-87 (1994)). For example, the following procedure is used for the screening of inhibitors with regard to the interaction between Grb2 - for example, full-length (sequence: see Lowenstein et al., Cell 70, 431-42 (1992)) or SH2 alone - and phosphorylated EGFR (full-length cytoplasmic tyrosine kinase or a fusion pro¬ duct obtained from Maltose Binding Protein and the carboxy-terminal part of the EGF recep¬ tor ("tail" EGFR-MBP fusion protein)) (for EGFR sequence, see Nature 309, 418-425 (1984); for purified recombinant intracellular domain (ICD), see Eur. J. Biochem. 207, 265-75 (1992); the EGFR-MBP fusion protein is made as follows: Oligonucleotides flanking the en¬ tire carboxy-terminal half (nucleotides 3112 to 3816) of the EGFR and containing enginee¬ red EcoRI-Hindlll restriction sites are used to amplify the appropriate DNA fragment by PCR. The amplified DNA fragment is recombined with purified EcoRI-Hindl I I-digested pMALc2 vector (New England Biolabs, Inc., Beverly, USA) downstream from and in the same reading frame as the malE gene, which encodes maltose-binding protein (MBP). The vector containing the fused gene is transformed in E. Coli, and the fusion protein is expres¬ sed from the P tac promoter. A crude cell extract is prepared and passed over a column of amylose resin. The fusion protein is then eluted with neutral buffer, containing maltose. Ali¬ quots are frozen in liquid nitrogen and stored at -70 °C). Wells of polystyrene microtiter plates (e.g. Nunc-lmmuno Plate MaxiSorp™) are coated ovemight at 4 °C in incubation buffer (20 mM Tris pH 7.5) with phosphorylated EGFR or "tail" EGFR-MBP fusion protein (phosphorylation conditions: 0.5 mg/ml of purified recombinant EGFR-ICD, or EGFR-MBP (+0.03mg/ml EGFR-ICD) is phosphorylated by the addition of 10 mM MnCI 2 , 10 mM MgCI 2 , 40 μM ATP in 20 mM Tris buffer pH 7.5 for 45 min). with a working solution containing 0.5 mg/ml of phosphorylated EGFR or MBP-EGFR. 11 ng/ml Grb2-SH2-GST [obtainable, e.g., from Santa Cruz Biotech, California, USA, or as follows: a cDNA clone encoding human Grb2 SH2 domain (e.g., aa 45-164) is amplified by polymerase chain reaction (PCR), using nucleotides with appropriate linkers, e.g. with BamHI (5').3' EcoRI linkers; the purified (e.g. BamHI -EcoRI) fragments from PCR products are then subcloned in-frame into the appropriate (e.g. BamHI -EcoRI) restriction sites of an appropriate vector (e.g. pGEX-3X, Pharmacia, Uppsala, Sweden) - comparable results are also obtained when using full length Grb2, see also Embo J. 13, 4011-21 (1994)] are then added to coated phosphorylated EGFR or "tail" EGFR-MBP fusion protein for 2 h at room temperature in the absence or presence of test substance of formula I dissolved in buffer ± dimethyl sulfoxide (maximally 25%). Bound SH2 is detected with polyclonal rabbit anti-GST antibody (obtained by immunisation of rabbits with glutathione-S-transferase) for 1 h at room temperature. Bound antibody is then detected after the addition of peroxydase- conjugated goat-antirabbit IgG (EIA Grade Affinity purified Goat Anti-Rabbit IgG (H+L) - Horseradish Peroxydase Conjugate from Bio-Rad, Hercules, USA) and incubation for 1 h at room temperature. Peroxydase activity is then monitored at 655 nm on a plate reader by the addition of a TMB substrate (Single Component TMB Peroxidase EIA Substrate Kit from Bio-Rad, Hercules, USA; TMB = 3,3',5,5'-tetramethylbenzidine solution). With this type of assay, IC S0 values (= the concentrations where half-maximal inhibition of the interaction is found) in the range of 10 "4 to 10 "10 M, preferably 10 "5 to 10 "10 M, more preferably in the range of 10 "6 to 10 "10 M) are found with test compounds of formula I. This type of assays is not limited to the EGF receptor - it can also be used analogously with erb-B2 or other protein tyrosine kinases. Furthermore, it is possible to use other SH2 domains instead of Grb2 SH2. For example, the interactions of the SH2-comprising proteins and phosphotyrosine comprising proteins mentioned above in the definition of a bivalent radical -(AA) n - in formula I as an analogue of an SH2 domain binding site of a protein with phosphotyrosine of a mammal can be tested. In addition, it can be shown by methods known in the art that injection of a compound of formula I into mammalian cells leads to a stop of cell growth (the test can be made in analogy to the well-known method of microinjection of antibodies into mammalian cells in which it has been shown that microinjection of antibodies against Grb2 blocks the induction of S phase entry in response to EGF and PDGF, see EMBO J. 12, 3467-73 (1993); or to the well-known methods for cell permeabilization where a) a phosphorylated peptide encompassing Tyr 716 (an autophosphorylation site) in the PDGFR kinase insert has been shown to significantly inhibit the activation of Ras by PDGF in permeabilized PAE cells as well as fibroblasts (see Mol. and Cell. Biol., 6715-26 (1994)). or b) the effect of various phosphopeptides on the activation of guanine nucleotide exchange on Ras by EGF and NGF has been studied in permeabilised 6-24 cells, the EGFR-Tyr 1068 phosphopeptide corresponding to an autophosphorylation site for Grb2 on the EGFR showing inhibition of EGF and NGF stimulation of Ras by 96% and 98%, respectively, at 50 μM concentration (Oncogene 9(12), 3483-3491 (1994)). The compounds of the invention, due to their ability to uncouple a phosphorylated protein, especially a protein tyrosine kinase, e.g. EGF receptor, from a respective SH2 containing protein, e.g. the SH2-containing Grb2, are able to inhibit subsequent cellular signal trans¬ duction pathways important for diseases such as viral, inflammatory, allergic, autoimmune, cardiovascular and especially proliferative diseases, such as for malignant hyperprolifera¬ tive diseases, e.g. tumor diseases, preferably breast cancer, chronic myelogenous leukemia (CML), thyroid carcinoma and osteosarcoma, or for hyperproliferation of epithelial cells, e.g. psoriasis, are appropriate for the treatment and prophylaxis of said diseases. Therefore, the compounds of the present invention are useful for the treatment of diseases that respond to inhibition of the interaction of (a) protein(s) comprising (an) SH2 domain(s) and a phosphoprotein, preferably a protein tyrosine kinase or a modified version thereof, more preferably of Grb2 SH2 with EGFR or modified derivatives thereof. The term "modified version" or "modified derivative" means mainly a derivative that is causative or active in the establishment of diseases, e.g. truncated versions, virus derived analogues, etc. The treatment can also, e.g. in the case of hematopoietic cell proliferative disorders, such as leukemias, be used in conjunction with autologous bone marrow transplantation and chemotherapy techniques. For example, an aliquot of bone marrow cells (even one cell or some single cells, which can be treated by microinjection of a compound of formula I as described above) are obtained from a patient, e.g. from the pelvis. The cells are then cultured in the presence of a compound of formula I (which may also be applied by microinjection) which is able to disrupt the protein tyrosine kinase/SH2-comprising protein- interaction. Thus blocking the signal transduction pathway of those bone marrow cells capable of forming complexes resulting from such interaction, it is possible to select against the presence of clonal daughter cells derived from these cells and to purge the culture(s) of these cells from those responsible for the hematopoietic cell proliferative disorder being treated. After chemotherapeutic and/or radiotherapeutic treatment of the patient from whom the cells have been obtained, the patient can receive an autologous infusion of cultured bone marrow cells resulting from the above purging procedure. Due to their high binding affinity to SH2 domains, such as those of Grb2, the compounds of formula I can also be bound covalently to chromatographic materials, thus making it possible to produce chromatographic materials for the affinity purification of natural or recombinant SH2-domains or SH2-comprising proteins from the cells of living organisms. For example, a compound of formula I with an appropriate free functional group (e.g. -NH 2 , -SH, -OH and/or -COOH) can be attached covalently to activated or activatable matrices appropriate for chromatography, e.g. cyanogen bromide activated matrices, epoxy-activated matrices, nitrophenyl chloroformate and N-hydroxysuccinimde chloroformate. polyacrylhydrazido agarose, oxirane acrylic beads, bromoacetyl-cellulose, epichlorohydrin- activated matrices, tresyl-chloride-activated agarose, vinylsuifone-activated agarose, and the like. Preferred activated or activatable coupling gels for affinity chromatography include but are not limited to a) for coupling of compounds of formula I with an -NH 2 group employed for binding: cyanogen bromide activated Sepharose 4B; ECH Sepharose 4B (carbodiimide coupling method used most often in analogy to process for preparation of compounds of formula I as described below); or activated CH Sepharose 4B; b) for coupling of compounds of formula I with an -NH 2 and/or an -SH group: Tresyl- activated Sepharose 4B; c) for coupling of compounds of formula I with an -NH 2 ,-OH and/or -SH group: epoxy- activated Sepharose 6B; and d) for coupling of compounds of formula I with a -COOH group: EAH Sepharose 4B (carbodiimide method for coupling most often used in analogy to process for preparation of compounds of formula I as described below). Sepharose stands for agarose derived chromatographic materials and is a trademark from Pharmacia, Uppsala, Sweden, from where the mentioned gels are available. In the following definitions of preferred compounds, general terms may be replaced by their more specific (more preferred) definitions as given above in order to obtain more preferred compounds. One preferred embodiment of the invention relates to a compound of formula I, wherein n is 1 to 15, X is arylcarbonyl, cycloalkylcarbonyl, arylsulfonyl, heterocyclylcarbonyl, heterocyclylsulfonyl; aryl-lower alkylcarbonyl, cycloalkyl-lower alkylcarbonyl, aryl-lower alkylsulfonyl, heterocyclyl- lower alkylcarbonyl, heterocyclyl-lower alkylsulfonyl with the proviso that in any of the lower alkyl radicals mentioned a methylene group may be replaced with oxa, aza or thia; or heterocyclyl-lower alkenylcarbonyl, PTI is the bivalent radical of phosphotyrosine or a phosphotyrosine mimic, AA stands for a bivalent radical of a natural or unnatural amino acid, and Y is hydroxy, a C-terminal protecting group or a primary, secondary or tertiary amino group, or a salt thereof if at least one salt-forming group is present. Preferred is a compound of formula I wherein n is 1 to 4, more preferably 1 to 3, most preferably 2 or especially 3; X is selected from (i) benzoyi or, even more preferably, from benzoyi substituted with amino; lower alkylamino; amino-lower alkyl; hydroxy; lower alkoxy; amino and hydroxy; amino and lower alkoxy; carboxy; lower-alkoxycarbonyl; cyano; halogen, especially chloro; lower-alkylthio; or lower alkylsulfinyl; especially from 4-aminobenzoyl, 3-aminobenzoyl, 2-aminobenzoyl, 4- lower alkylamino-benzoyl, such as 4-methylamino-benzoyl, 4-(amino-lower alkyl)-benzoyl, such as 4-(methylamino)-benzoyl, 4-hydroxy-benzoyl, 4-lower alkoxy-, such as 4- methoxybenzoyl, 4-amino-2-hydroxy-benzoyl, 4-amino-3-lower alkoxy-benzoyl, such as 4- amino-3-methoxy-benzoyl, 4-carboxybenzoyl, 4-lower alkoxycarbonyl-benzoyl, such as 4- methoxycarbonyl-benzoyl, 4-cyanobenzoyl, 4-lower alkylthio-benzoyl, such as 4- methylthiobenzoyl, 4-lower alkylsulfinyl-benzoyl, such as 4-lower methylsulfinyl-benzoyi; and most preferably from 3- or especially 4-aminobenzoyl; (ii) naphthoyl or hydroxy-naphthoyl, such as naphthalene-2-yl-carbonyl or especially 6- hydroxy-naphthalene-2-yl-carbonyl, or (less preferably) fluorenylcarbonyl, such as fluoren-9- ylcarbonyl; (iii) cyclohexylcarbonyl or especially 1 ,2,3,4-tetrahydronaphthyl-2-carbonyl (iv) tricyclo[5.2.1.0 2,6 ]dec-8-ylcarbonyi or especially adamantoyl, preferably 1-adamantoyl ...(v) pyridylcarbonyl which is unsubstituted or substituted with amino, such as pyridin-4-yl- or pyridin-3-ylcarbonyl, or amino-pyridin-3-yl-carbonyl, such as 2- or 6-amino-pyridin-3- ylcarbonyl, benzimidazolylcarbonyl, such as benzimidazol-5-ylcarbonyl, quinolinyl-carbonyl, such as quinoline-2-, quinoline-3- or quinoline-6-ylcarbonyl, 2,3-dihydrobenzofuranylcar- bonyl, such as 2,3-dihydrobenzofuran-5-ylcarbonyl, or indolylcarbonyl, such as indole-5-yl-, indole-3-yl- or indole-2-yl-carbonyl; most preferably from quinoline-6-ylcarbonyi and especially from indolylcarbonyl, such as indole-3- and indole-5-ylcarbonyl; (vi) chromenylcarbonyl, such as 2H-chromen-3-ylcarbonyl, that is unsubstituted by 1 to 3 substitutents selected from oxo and hydroxy, especially 7,8-dihydroxy-2-oxo-2H- (benzopyran)-3-yl-carbonyl; (vii) carbamoyl-lower alkanoyl, wherein lower alkanoyl is especially propionyl, especially 3- carbamoylpropionyl; (vii) phenyl-methoxycarbonyl wherein the phenyl residue is unsubstituted or substituted with amino in the (in growing preference) 2-, 3- and 5-, 4- or 3-position of the phenyl ring; (±)-, (+) or (-)-1-(3-aminophenyl)ethyloxycarbonyl; hydroxybenzyloxy- or hydroxyphenyl-2- ethoxycarbonyl, such as 3-hydroxybenzyloxycarbonyl or 3-hydroxyphenyl-2-ethoxy- carbonyl; (with less preference) lower alkanoylamino-phenyloxymethylcarbonyl, such as 2-, 3- or especially 4-acetylaminophenyloxymethylcarbonyl, aminophenyloxymethylcarbonyl, such as 3- or 4-aminophenyloxycarbonyl; aminophenyl-lower alkylcarbonyl, such as 4- aminophenyl-acetyl or 3-(3-aminophenyi)-propionyl; or (with still less preference) benzyl¬ oxycarbonyl or phenylacetyl; (viii) dihydroxyphenyl-lower alkylcarbonyl, especially 3-(3,4-dihydroxyphenyl)-propionyl or 2-(3,4-dihydroxyphenyl)-acetyl; (ix) cyclohexyl-lower alkylcarbonyl, especially 3-(cyclohexyl)-propionyl; (x) unsubstituted or lower alkyl-substituted 2-(thiazolyl)-ethoxycarbonyl, such as 2-(4- methyl-thiazol-5-yl)ethoxycarbonyl, unsubstituted or amino-substituted thiazolyl-lower alkylcarbonyl, such as 2-amino-thiazole-5-ylacetyl, or especially indolyl-lower alkylcarbonyl, such as indole-3-yl-acetyl, 3-(indole-3-yl)propionyl or 4-(indole-3-yl)butyroyl; (xi) imidazolyl-lower alkenylcarbonyl, such as imidazole-4-yl-lower alkenylcarbonyl, especially imidazole-4-yl-acryloyl, or indolyl-lower alkenylcarbonyl, such as indole-3-yl- acryloyl; (xii) cinnamoyl substituted by 1 to 2 moieties selected independently from methoxy and especially hydroxy, especially p-hydroxycinnamoyl, m-hydroxy-p-methoxy-cinnamoyl or preferably m,p-dihydroxy-cinnamoyl; and (xiii) if Y is secondary or tertiary amino, also from lower alkanoyl, especially acetyl, PTI is a bivalent radical of tyrosine or (preferably) a bivalent radical of phosphotyrosine (in the D-, L- or less preferably the (D.L)-form) or of a phosphotyrosine mimic in the form of a bivalent radical (which is bound N-terminally via the imino group resulting from the α-amino group and C-terminally via the carbonyl group resulting from its α-carboxy group) of an amino acid selected from phosphonomethyl-phenylalanine, especially 4-phosphono-methyl- phenylalanine, phosphono-(α-fluoro)methyl-phenylalanine, especially 4-phosphono-(α- fluoro)methyl-phenylalanine, phosphono-(α,α-difluoro)methyl-phenylalanine, especially 4- phosphono-(α,α-dif luoro) methyl-phenylalanine, phosphono-(α-hydroxy)methyl-phenyl- alanine, especially 4-phosphono-(α-hydroxy)methyl-phenylalanine, O-sulfo-tyrosine, such as 4-(O-sulfo)tyrosine, dicarboxymethoxy-phenylalanine (= (HOOC) 2 -CH 2 -O-phenylalanine , especially 4-(dicarboxymethoxy)-phenylalanine aspartic acid, glutamic acid, phosphosenne and phosphothreonine, each of which is present in the (D,L)-, D- or preferably the L-form; -(AA) n - has one of the following meanings: • A bivalent radical of a tripeptide of the formula -(AA 1 )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is preferably selected from -He-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly- and -Phe- or (alternatively or in addition to the group of moieties mentioned just before) from -Ac 7 c-, -Nbo-, -Met-, -Pro-, -βAla-, -Gin-, -Glu-, -DHph-, -HPh- and -tLe-, most preferably -He-, -Ac 5 c-, -Ac 6 c-, -Asp- or -Gly- or (alternatively or in addition to the group of moieties mentioned just before) - AC T C-, -Nbo- and -Gin-; -(AA 2 )- is preferably selected from -Asn-, and also from -βAla- and -Gly-, or (altematively or in addition to the group of moieties mentioned just before), from -lie-, -βAla- and Gin; most preferably -Asn-; and -(AA 3 )- is preferably selected from -Val-, and -β-Ala, and also from -Gly-, -Gin-, -Val-, -Asp- and -Ac 5 c- ; or, less preferably, • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- and -(AA 2 )- preferably have the meanings given above, preferably -(AA 1 )- being -Ile- or -Ac 6 c-, or (alternatively or in addition to the group of moieties mentioned just before) -Ac^-, -Nbo- and -Gin-; and -(AA 2 )- being -Asn- (preferred) or also -βAla-; • or (even less preferably) simply a bivalent radical of an amino acid selected from the amino acids mentioned above, especially -Ile- or (alternatively or in addition to the group of moieties mentioned just before) -Ac 6 c-, -Nbo- and Ac 5 c-; and Y is amino (-NH 2 ) or monosubstituted amino selected from lower alkylamino, such as methylamino, ethylamino; isobutylamino or 3-methylbutylamino; octylamino, such as 2-ethyl- hexyl-amino; aryloxy-lower alkylamino, especially halonaphthyloxy-lower alkylamino, such as 2-(1-bromo-naphthalen-2-yloxy)-ethylamino, or naphthyloxy-lower alkylamino, such as 2- (naphthalen-2-yloxy or naphthalen-1-yloxy)-ethylamino; aryl-lower alkylamino, such as phenyl-lower alkylamino, e.g. benzylamino, 3-phenylpropylamino, di-phenyl-lower alkylamino, such as 2,2-diphenyl-ethylamino or 3,3-diphenyl-propylamino, (mono- or di-halo- phenyl)-lower alkylamino, such as 2-(4-chlorophenyl)ethylamino or 3-(2,4-dichlorophenyl)- propylamino, naphthalenyl-lower alkylamino, such as 3-naphthtalen-1 -ylpropylamino or 3- naphthalen-2-ylpropylamino, hydroxy-naphthalenyl-lower alkylamino, such as 3-(2-hydroxy- naphthalen-1-yl)-propylamino, or phenanthrenyl-lower alkylamino, such as 3-phenanthren- 9-yl-propylamino; cycloalkylamino, such as cyclohexylamino; and cycloalkyl-lower alkylamino, such as cyclohexylmethylamino; or a salt thereof where at least one salt-forming group is present. Preferred is also a compound of formula I wherein n is 1 to 4, more preferably 1 to 3, most preferably 2 or especially 3; X is selected from (i) benzoyi or, even more preferably, from benzoyi substituted with amino; lower alkylamino; amino-lower alkyl; hydroxy; lower alkoxy; amino and hydroxy; amino and lower alkoxy; carboxy; lower-alkoxycarbonyl; cyanc; halogen, especially chloro; lower-alkylthio; or lower alkylsulfinyl; especially from 4-aminobenzoyl, 3-ami no benzoyi, 2-aminobenzoyl, 4- lower alkylamino-benzoyl, such as 4-methylamino-benzoyl, 4-(amino-lower alkyl)-benzoyl, such as 4-(methylamino)-benzoyl, 4-hydroxy-benzoyl, 4-lower alkoxy-, such as 4- methoxybenzoyl, 4-amino-2-hydroxy-benzoyl, 4-amino-3-lower alkoxy-benzoyl, such as 4- amino-3-methoxy-benzoyl, 4-carboxybenzoyl, 4-lower alkoxycarbonyl-benzoyl, such as 4- methoxycarbonyl-benzoyl, 4-cyanobenzoyl, 4-lower alkylthio-benzoyl, such as 4- methylthiobenzoyl, 4-lower alkylsulfinyl-benzoyl, such as 4-lower methylsulfinyl-benzoyi; and most preferably from 3- or especially 4-aminobenzoyl; (ii) pyridylcarbonyl which is unsubstituted or substituted with amino, such as pyridin-4-yl- or pyridin-3-ylcarbonyl, or amino-pyridin-3-yl-carbonyl, such as 2- or 6-amino-pyridin-3- ylcarbonyl, benzimidazolylcarbonyl, such as benzimidazol-5-ylcarbonyl, quinolinyl-carbonyl, such as quinoline-2-, quinoline-3- or quinoline-6-ylcarbonyl, 2,3-dihydrobenzofuranyl- carbonyl, such as 2,3-dihydrobenzofuran-5-ylcarbonyl, or indolylcarbonyl, such as indole-5- yl-, indole-3-yl- or indole-2-yl-carbonyl; most preferably from quinoline-6-ylcarbonyl and especially from indolylcarbonyl, such as indole-3- and indole-5-yicarbonyl; (iii) phenyl-methoxycarbonyl wherein the phenyl residue is unsubstituted or substituted with amino in the (in growing preference) 2-, 3- and 5-, 4- or 3-position of the phenyl ring; (±)-, (+) or (-)-1 -(3-aminophenyl)ethyloxycarbonyl; hydroxybenzyloxy- or hydroxyphenyl-2- ethoxycarbonyl, such as 3-hydroxybenzyloxycarbonyl or 3-hydroxyphenyl-2-ethoxy- carbonyl; (with less preference) lower alkanoylamino-phenyioxymethylcarbonyl, such as 2-, 3- or especially 4-acetylaminophenyloxymethylcarbonyl, aminophenyloxymethylcarbonyl, such as 3- or 4-aminophenyioxycarbonyl; aminophenyl-lower alkylcarbonyl, such as 4- aminophenyl-acetyl or 3-(3-aminophenyl)-propionyl; and (with still less preference) benzyl¬ oxycarbonyl or phenylacetyl; (iv) unsubstituted or lower alkyl-substituted 2-(thiazolyl)-ethoxycarbonyl, such as 2-(4- methyl-thiazol-5-yl)ethoxycarbonyl, unsubstituted or amino-substituted thiazolyl-lower alkylcarbonyl, such as 2-amino-thiazole-5-ylacetyl, or especially indolyl-lower alkylcarbonyl, such as indole-3-yl-acetyl, 3-(indole-3-yl)propionyl or 4-(indole-3-yl)butyroyl; and (v) imidazolyl-lower alkenylcarbonyl, such as imidazole-4-yl-lower alkenylcarbonyl, especially imidazole-4-yl-acryloyl, or indolyl-lower alkenylcarbonyl, such as indole-3-yl- acryloyl; PTI is a bivalent radical of phosphotyrosine (in the D-, L- or less preferably the (D,L)-form) or of a phosphotyrosine mimic in the form of a bivalent radical (which is bound N-terminally via the imino group resulting from the α-amino group and C-terminally via the carbonyl group resulting from its α-carboxy group) of an amino acid selected from phosphonomethyl- phenylalanine, especially 4-phosphono-methyl-phenylalanine, phosphono-(α-fluoro)methyl- phenylalanine, especially 4-phosphono-(α-fiuoro)methyl-phenylalanine, phosphono-(α,α- difluoro)methyl-phenylalanine, especially 4-phosphono-(α,α-difluoro)methyl-phenylalanine, phosphono-(α-hydroxy)methyl-phenylalanine, especially 4-phosphono-(α-hydroxy)methyl- phenylalanine, O-sulfo-tyrosine, such as 4-(O-sulfo)tyrosine, dicarboxymethoxy- phenylalanine (= (HOOC) 2 -CH 2 -O-phenylalanine , especially 4-(dicarboxymethoxy)- phenylalanine aspartic acid, glutamic acid, phosphoserine and phosphothreonine, each of which is present in the (D,L)-, D- or preferably the L-form; -(AA) n - has one of the following meanings: • A bivalent radical of a tripeptide of the formula -(AA 1 )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is pre¬ ferably selected from -He-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly- and -Phe-, most preferably -lie-, -Ac 5 c-, -Ac 6 c-, -Asp- or -Gly-; -(AA 2 )- is preferably selected from -Asn-, and also from - βAla- and -Gly-, most preferably -Asn-; and -(AA 3 )- is preferably selected from -Val-, and -β-Ala, and also from -Gly-, -Gin-, -Val-, -Asp- and -Ac 5 c- ; • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- and -(AA 2 )- preferably have the meanings given above, preferably -(AA 1 )- being -Ile- or -Ac 6 c- and -(AA 2 )- being -Asn- (preferred) or also -βAia-; • or (less preferably) simply a bivalent radical of an amino acid selected from the amino acids mentioned above, especially -He-; and Y is a free amino group (preferred), a mono- or disubstituted amino group the substituents of which are preferably selected from the group comprising lower alkyl, e.g. methyl or ethyl, phenyl-lower alkyl, e.g. benzyl, pyrrolidinyl-lower alkyl, e.g. 2-(1-pyrrolidinyl)-ethyl, pyridyl- lower alkyl, e.g. 2-(2-pyridyl)-ethyl, furyl-lower alkyl, e.g. 2-furylmethyl, morpholinyl-lower alkyl, e.g. 2-(4-morpholinyl)-ethyl, and indolyl-lower alkyl, e.g. 2-(3-indolyl)-ethyl; or is 1- pyrrolidinyl or 4-morphoiinyl, or a salt thereof. Preferred is also a compound of formula I wherein n is 1 to 4, more preferably 1 to 3, most preferably 2 or especially 3; X is selected from (i) naphthoyl or hydroxy-naphthoyl, such as naphthalene-2-yl-carbonyl or especially 6- hydroxy-naphthalene-2-yl-carbonyl, or (less preferably) fluorenylcarbonyl, such as fluoren-9- ylcarbonyl; (ii) cyclohexylcarbonyl or especially 1 ,2,3,4-tetrahydronaphthyl-2-carbonyl (iii) tricyclo[5.2.1.0 2,6 ]dec-8-ylcarbonyl or especially adamantoyl, preferably 1-adamantoyl (iv) chromenylcarbonyl, such as 2H-chromen-3-ylcarbonyl, that is unsubstituted by 1 to 3 substitutents selected from oxo and hydroxy, especially 7,8-dihydroxy-2-oxo-2H- (benzopyran)-3-yl-carbonyl; (v) carbamoyl-lower alkanoyl, wherein lower alkanoyl is especially propionyl, especially 3- carbamoylpropionyl; (vi) dihydroxyphenyl-lower alkylcarbonyl, especially 3-(3,4-dihydroxyphenyl)-propionyl or 2-(3,4-dihydroxyphenyl)-acetyl; (vii) cyclohexyl-lower alkylcarbonyl, especially 3-(cyclohexyl)-propionyl; and (viii) cinnamoyl substituted by 1 to 2 moieties selected independently from methoxy and especially hydroxy, especially p-hydroxycinnamoyl, m-hydroxy-p-methoxy-cinnamoyl or preferably m,p-dihydroxy-cinnamoyl; and (ix) if Y is secondary or tertiary amino, also from lower alkanoyl, especially acetyl, PTI is a bivalent radical of tyrosine or (preferably) a bivalent radical of phosphotyrosine (in the D-, L- or less preferably the (D,L)-form) or of a phosphotyrosine mimic in the form of a bivalent radical (which is bound N-terminally via the imino group resulting from the α-amino group and C-terminally via the carbonyl group resulting from its α-carboxy group) of an amino acid selected from phosphonomethyl-phenylalanine, especially 4-phosphono-methyl- phenylalanine, phosphono-(α-fluoro)methyl-phenylalanine, especially 4-phosphono-(α- fluoro)methyl-phenylalanine, phosphono-(α,α-difluoro)methyi-phenylalanine, especially 4- phosphono-(α,α-difluoro)methyl-phenylalanine, phosphono-(α-hydroxy)methyl-phenyl- alanine, especially 4-phosphono-(α-hydroxy)methyl-phenylalanine, O-sulfo-tyrosine, such as 4-(O-sulfo)tyrosine, dicarboxymethoxy-phenylalanine (= (HOOC) 2 -CH 2 -O-phenylalanine , especially 4-(dicarboxymethoxy)-phenylalanine aspartic acid, glutamic acid, phosphoserine and phosphothreonine, each of which is present in the (D,L)-, D- or preferably the L-form; -(AA)n- has one of the following meanings: • A bivalent radical of a tripeptide of the formula -(AA 1 )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is preferably selected from -He-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly- and -Phe- or (altematively or in addition to the group of moieties mentioned just before) from -AC7C-, -Nbo-, -Met-, -Pro-, -βAla-, -Gin-, -Glu-, -DHph-, -HPh- and -tLe-, most preferably -He-, -Ac 5 c-, -Ac 6 c-, -Asp- or -Gly- or (altematively or in addition to the group of moieties mentioned just before) - Ac 7 c-, -Nbo- and -Gin-; -(AA 2 )- is preferably selected from -Asn-, and also from -βAla- and -Gly-, or (alternatively or in addition to the group of moieties mentioned just before), from -lie-, -βAla- and Gin; most preferably -Asn-; and -(AA 3 )- is preferably selected from -Val-, and -β-Ala, and also from -Gly-, -Gin-, -Val-, -Asp- and -Ac 5 c- ; or, less preferably, • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- and -(AA 2 )- preferably have the meanings given above, preferably -(AA 1 )- being -lie- or -Ac 6 c-, or (altematively or in addition to the group of moieties mentioned just before) -AC 7 C-, -Nbo- and -Gin-; and -(AA 2 )- being -Asn- (preferred) or also -βAla-; • or (even less preferably) simply a bivalent radical of an amino acid selected from the amino acids mentioned above, especially -Ile- or (altematively or in addition to the group of moieties mentioned just before) -Ac 6 c-, -Nbo- and Ac 5 c-, and Y is amino (-NH 2 ) or monosubstituted amino selected from lower alkylamino, such as methylamino, ethylamino; isobutylamino or 3-methylbutylamino; octylamino, such as 2-ethyl- hexyl-amino; aryloxy-lower alkylamino, especially halonaphthyloxy-lower alkylamino, such as 2-(1-bromo-naphthalen-2-yloxy)-ethylamino, or naphthyloxy-lower alkylamino, such as 2- (naphthalen-2-yloxy or naphthalen-1 -yloxy)-ethylamino; aryl-lower alkylamino, such as phenyl-lower alkylamino, e.g. benzylamino, 3-phenylpropylamino, di-phenyl-lower alkylamino, such as 2,2-diphenyl-ethylamino or 3,3-diphenyl-propylamino, (mono- or di-halo- phenyl)-lower alkylamino, such as 2-(4-chlorophenyl)ethylamino or 3-(2,4-dichlorophenyl)- propylamino, naphthalenyl-lower alkylamino, such as 3-naphthtalen-1 -ylpropylamino or 3- naphthalen-2-ylpropylamino, hydroxy-naphthalenyl-lower alkylamino, such as 3-(2-hydroxy- naphthalen-1-yl)-propylamino, or phenanthrenyl-lower alkylamino, such as 3-phenanthren- 9-yl-propylamino; cycloalkylamino, such as cyclohexylamino; and cycloalkyl-lower alkylamino, such as cyclohexylmethylamino; or a salt thereof where at least one salt-forming group is present. More preferred is a compound of formula I wherein n is 1 , 2 or 3, especially 2 or 3; X is selected from 4-aminobenzoyl, 3-aminobenzoyl, 4-amino-2-hydroxy-benzoyl, 4-lower alkoxycarbonyl-benzoyl, such as 4-methoxycarbonyl-benzoyl, quinolinyl-carbonyl, such as quinoline-2-, quinoline-3- or quinoiine-6-ylcarbonyl, indolylcarbonyl, such as indole-5-yi-, indole-3-yl- or indole-2-yi-carbonyl; phenyl-methoxycarbonyl wherein the phenyl residue is unsubstituted or substituted with amino in the (in growing preference) 2-, 3- and 5-, 4- or 3- position of the phenyl ring; (±)-, (+) or (-)-1-(3-aminophenyl)ethyloxycarbonyl; hydroxy- benzyloxy- or hydroxyphenyl-2-ethoxycarbonyl, such as 3-hydroxybenzyloxycarbonyl or 3- hydroxyphenyl-2-ethoxy-carbonyl; unsubstituted or lower alkyl-substituted 2-(thiazoiyl)- ethoxycarbonyl, such as 2-(4-methyl-thiazol-5-yl)ethoxycarbonyl, unsubstituted or amino- substituted thiazolyl-lower alkylcarbonyl, such as 2-amino-thiazole-5-ylacetyl, indolyl-lower alkylcarbonyl, such as indole-3-yl-acetyl, 3-(indole-3-yl)propionyl or 4-(indole-3-yl)-butyroyl, naphthoyl or hydroxy-naphthoyi, such as naphthalene-2-yl-carbonyl or especially 6-hydroxy- naphthalene-2-yl-carbonyl, cyclohexylcarbonyl, 1 ,2,3,4-tetrahydronaphthyl-2-carbonyl (preferred), adamantoyl, preferably 1-adamantoyl, 7,8-dihydroxy-2-oxo-2H-(benzopyran)-3- yl-carbonyl, carbamoyl-lower alkanoyl, especially 3-carbamoylpropionyl, dihydroxyphenyl- lower alkylcarbonyl, especially 3-(3,4-dihydroxyphenyl)-propionyl or 2-(3,4-dihydroxyphenyl)- acetyl, and cinnamoyl substituted by 1 to 2 moieties selected independently from methoxy and especially hydroxy, especially p-hydroxycinnamoyl, m-hydroxy-p-methoxy-cinnamoyl or preferably m,p-dihydroxy-cinnamoyl; and, if Y is monosubstituted amino, also from lower alkanoyl, especially acetyl; PTI is a bivalent radical of phosphotyrosine (in the D-, L- (most preferred) or (less preferably) the (D,L)-form) or of a phosphotyrosine mimic of the phosphono-(α,α- difluoro)methyl-phenylalanine or the phosphonomethyl-phenylalanine type, especially 4- phosphono-(α,α-difiuoro)methyl-phenylalanine -(AA) n - has one of the following meanings: • A bivalent radical of a tripeptide of the formula -(AA 1 )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is preferably selected from -He-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly- and -Phe- or (altematively or in addition to the group of moieties mentioned just before) from -AC7C-, -Nbo-, -Met-, -Pro-, -βAla-, -Gin-, -Glu-, -DHph-, -HPh- and -tLe-, most preferably -He-, -Ac 5 c-, -Ac 6 c-, -Asp- or -Gly- or (alternatively or in addition to the group of moieties mentioned just before) - Ac/C-, -Nbo- and -Gin-; -(AA 2 )- is preferably selected from -Asn-, and also from -βAla- and -Gly-, or (altematively or in addition to the group of moieties mentioned just before), from -He-, -βAia- and Gin; most preferably -Asn-; and -(AA 3 )- is preferably selected from -Val-, and -β-Ala, and also from -Gly-, -Gin-, -Val-, -Asp- and -Ac 5 c- ; or, less preferably, • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- and -(AA 2 )- preferably have the meanings given above, preferably -(AA 1 )- being -lie- or -Ac 6 c-, or (altematively or in addition to the group of moieties mentioned just before) -Ac 7 c-, -Nbo- and -Gin-; and -(AA 2 )- being -Asn- (preferred) or also -βAla-; • or (even less preferably) simply a bivalent radical of an amino acid selected from the amino acids mentioned above, especially -lie- or (alternatively or in addition to the group of moieties mentioned just before) -Ac 6 c-, -Nbo- and Ac 5 c-, and Y is amino (-NH 2 ) or monosubstituted amino selected from lower alkylamino, such as methylamino, ethylamino; isobutylamino or 3-methylbutylamino; octylamino, such as 2-ethyl- hexyl-amino; aryloxy-lower alkylamino, especially halonaphthyloxy-lower alkylamino, such as 2-(1-bromo-naphthalen-2-yloxy)-ethylamino, or naphthyloxy-lower alkylamino, such as 2- (naphthalen-2-yloxy or naphthalen-1 -yloxy)-ethylamino; aryl-lower alkylamino, such as phenyl-lower alkylamino, e.g. benzylamino, 3-phenylpropylamino, di-phenyl-lower alkylamino, such as 2,2-diphenyl-ethylamino or 3,3-diphenyl-propylamino, (mono- or di-halo- phenyl)-lower alkylamino, such as 2-(4-chlorophenyl)ethylamino or 3-(2,4-dichlorophenyl)- propylamino, naphthalenyl-lower alkylamino, such as 3-naphthtalen-1 -ylpropylamino or 3- naphthalen-2-ylpropylamino, hydroxy-naphthalenyl-lower alkylamino, such as 3-(2-hydroxy- naphthalen-1-yl)-propylamino, or phenanthrenyl-lower alkylamino, such as 3-phenanthren- 9-yl-propylamino; cycloalkylamino, such as cyclohexylamino; and cycloalkyl-lower alkylamino, such as cyclohexylmethylamino; or a salt thereof where at least one salt-forming group is present. More preferred is also a compound of formula I wherein n is 2 or 3; X is selected from 4-aminobenzoyl, 3-aminobenzoyl, 4-amino-2-hydroxy-benzoyl, 4-lower alkoxycarbonyl-benzoyl, such as 4-methoxycarbonyl-benzoyl, quinolinyl-carbonyl, such as quinoliπe-2-, quinoline-3- or quinoline-6-ylcarbonyl, indolylcarbonyl, such as indole-5-yl-, indole-3-yl- or indole-2-yl-carbonyl; phenyl-methoxycarbonyl wherein the phenyl residue is unsubstituted or substituted with amino in the (in growing preference) 2-, 3- and 5-, 4- or 3- position of the phenyl ring; (±)-, (+) or (-)-1-(3-aminophenyl)ethyloxycarbonyl; hydroxy- benzyloxy- or hydroxyphenyl-2-ethoxycarbonyl, such as 3-hydroxybenzyloxycarbonyl or 3- hydroxyphenyl-2-ethoxy-carbonyl; unsubstituted or lower alkyl-substituted 2-(thiazolyl)- ethoxycarbonyl, such as 2-(4-methyl-thiazol-5-yl)ethoxycarbonyl, unsubstituted or amino- substituted thiazolyl-lower alkylcarbonyl, such as 2-amino-thiazole-5-ylacetyi, and indolyl- lower alkylcarbonyl, such as indole-3-yl-acetyl, 3-(indole-3-yl)propionyl or 4-(indole-3-yl)- butyroyl; PTI is a bivalent radical of phosphotyrosine (in the D-, L- (most preferred) or (less preferably) the (D,L)-form) or of a phosphotyrosine mimic of the phosphono-(α,α- difluoro)methyl-phenylalanine type, especially 4-phosphono-(α,α-difluoro)methyl- phenylalanine -(AA) n - has one of the following meanings: • a bivalent radical of a tripeptide of the formula -(AA 1 )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is selected from -He-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly- and -Phe-, most preferably -lie-, -Ac 5 c-, -Ac 6 c-, -Asp- or -Gly-; -(AA 2 )- is selected from -Asn-, and also from -βAla- and -Gly-, most preferably -Asn-; and -(AA 3 )- is selected from -Val-, and -β-Ala, and also from -Gly-, -Gin-, -Val-, -Asp- and -Ac 5 c- ; or • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- is-lle- or -Ac 6 c- and -(AA 2 )- is-Asn- (preferred) or also -βAla-; and Y is a free amino group (-NH 2 ), or a salt thereof. More preferred is also a compound of formula i wherein n is 1 , 2 or 3, especially 2 or 3; X is selected from naphthoyl or hydroxy-naphthoyi, such as naphthalene-2-yl-carbonyl or especially 6-hydroxy-naphthalene-2-yl-carbonyl, cyclohexylcarbonyl, 1 ,2,3,4- tetrahydronaphthyl-2-carbonyl (preferred), adamantoyl, preferably 1-adamantoyl, 7,8- dihydroxy-2-oxo-2H-(benzopyran)-3-yl-carbonyl, carbamoyl-lower alkanoyl, especially 3- carbamoylpropionyl, dihydroxyphenyl-lower alkylcarbonyl, especially 3-(3,4- dihydroxyphenyl)-propionyl or 2-(3,4-dihydroxyphenyl)-acetyl, and cinnamoyi substituted by 1 to 2 moieties selected independently from methoxy and especially hydroxy, especially p- hydroxycinnamoyl, m-hydroxy-p-methoxy-cinnamoyl or preferably m.p-dihydroxy-cinnamoyl; and, if Y is monosubstituted amino, also from lower alkanoyl, especially acetyl; PTI is a bivalent radical of phosphotyrosine (in the D-, L- (most preferred) or (less preferably) the (D,L)-form) or of a phosphotyrosine mimic of the phosphono-(α,α- difluoro)methyl-phenylalanine or the phosphonomethyl-phenylalanine type, especially 4- phosphono-(α,α-difluoro)methyl-phenylalanine -(AA) n - has one of the following meanings: • A bivalent radical of a tripeptide of the formula -(AA 1 )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is preferably selected from -He-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly- and -Phe- or (alternatively or in addition to the group of moieties mentioned just before) from -AC T C-, -Nbo-, -Met-, -Pro-, -βAla-, -Gin-, -Glu-, -DHph-, -HPh- and -tLe-, most preferably -He-, -Ac 5 c-, -Ac 6 c-, -Asp- or -Gly- or (alternatively or in addition to the group of moieties mentioned just before) - Ac^-, -Nbo- and -Gin-; -(AA 2 )- is preferably selected from -Asn-, and also from -βAla- and -Gly-, or (alternatively or in addition to the group of moieties mentioned just before), from -He-, -βAla- and Gin; most preferably -Asn-; and -(AA 3 )- is preferably selected from -Val-, and -β-Ala, and also from -Gly-, -Gin-, -Vai-, -Asp- and -Ac 5 c- ; or, less preferably, • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- and -(AA 2 )- preferably have the meanings given above, preferably -(AA 1 )- being -He- or -Ac 6 c-, or (altematively or in addition to the group of moieties mentioned just before) -Ac^-, -Nbo- and -Gin-; and -(AA 2 )- being -Asn- (preferred) or also -βAla-; • or (even less preferably) simply a bivalent radical of an amino acid selected from the amino acids mentioned above, especially -lie- or (alternatively or in addition to the group of moieties mentioned just before) -Ac 6 c-, -Nbo- and Ac 5 c-, and Y is monosubstituted amino selected from lower alkylamino, such as methylamino, ethylamino; isobutylamino or 3-methylbutylamino; octylamino, such as 2-ethyl-hexyl-amino; aryloxy-lower alkylamino, especially halonaphthyloxy-lower alkylamino, such as 2-(1 -bromo- naphthalen-2-yloxy)-ethylamino, or naphthyloxy-lower alkylamino, such as 2-(naphthalen-2- yloxy or naphthalen-1-yloxy)-ethylamino; aryl-lower alkylamino, such as phenyl-lower alkylamino, e.g. benzylamino, 3-phenylpropylamino, di-phenyl-lower alkylamino, such as 2,2-diphenyl-ethylamino or 3,3-diphenyl-propylamino, (mono- or di-halo-phenyl)-lower alkyl¬ amino, such as 2-(4-chlorophenyl)ethylamino or 3-(2,4-dichlorophenyl)-propylamino, naphthalenyl-lower alkylamino, such as 3-naphthtalen-1-ylpropylamino or 3-naphthalen-2- ylpropylamino, hydroxy-naphthalenyl-lower alkylamino, such as 3-(2-hydroxy-naphthalen-1- yl)-propylamino, or phenanthrenyl-lower alkylamino, such as 3-phenanthren-9-yl- propylamino; cycloalkylamino, such as cyclohexylamino; and cycloalkyl-lower alkylamino, such as cyclohexylmethylamino; or a salt thereof where at least one salt-forming group is present. Especially preferred is a compound mentioned in the examples, or a (preferably pharmaceutically acceptable) salt thereof. Most preferred is a compound of formula I being selected from the following compounds: 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 3), 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-Ac5C-Asn-Gln-NH2 (SEQ ID NO: 6), 3-aminobenzyloxycarbonyl-Tyr(PO3H2)-Acgc-Asn-Gln-NH2 (SEQ ID NO: 7), 4-aminobenzoyl-Tyr(Pθ3H2)-He-Asn-Gin-NH2 (SEQ ID NO: 24), 4-aminobenzoyl-Tyr(Pθ3H2)-Asp-Asn-Gln-NH2 (SEQ ID NO: 51), 4-aminobenzoyl-Tyr(PO3H2)-Gly-Asn-Gln-NH2 (SEQ ID NO: 52), 4-aminobenzoyl-Tyr(Pθ3H2)-He-Asn-βAla-NH2 (SEQ ID NO: 58), lndole-5-ylcarbonyl-Tyr(PO 3 H2)-He-Asn-Gln-NH2 (SEQ ID NO: 61) lndole-5-ylcarbonyI-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 62) lndole-5-ylcarbonyl-Tyr(Pθ3H2)-Ac6C-Asn-Gln-NH2 (SEQ ID NO: 63); and 3-aminobenzyloxycarbonyl-L-F2Pmp-lle-Asn-Gln-NH2 (SEQ ID NO: 64) Most preferred is also a compound of formula I being selected from the following compounds: trans-3,4-dihydroxy-cinnamoyl-Tyr(Pθ3H2)-He-NH2 (SEQ ID NO: 70); trans-3,4-dihydroxy-cinnamoyl-Tyr(Pθ3H2)-Ac6C-NH2 (SEQ ID NO: 71); trans-3,4-dihydroxy-cinnamόyl-Tyr(Pθ3H2)-Ac6C-Asn-NH2 (SEQ ID NO: 72) (very preferred); trans-3,4-dihydroxy-cinnamoyl-Tyr(Pθ3H2)-Met-Asn-NH2 (SEQ ID NO: 74) (very preferred); 3-(3,4-dihydroxyphenyl)-propionyl-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 76); 3,4-dihydroxyphenyl-acetyl-Tyr(PO3H2)-lle-Asn-NH2 (SEQ ID NO: 77); trans-3,4-dihydroxy-cinnamoyl-Tyr(Pθ3H2)-Ac7C-Asn-NH2 (SEQ ID NO: 80) (very preferred); trans-3,4-dihydroxy-cinnamoyl-Tyr(PO3H2)-Nbo-Asn-NH2 (SEQ ID NO: 81) (very preferred); trans-3,4-dihydroxy-cinnamoyl-Tyr(Pθ3H2)-Nbo-NH2 (epimer 1) (SEQ ID NO: 82); trans-3,4-dihydroxy-cinnamoyl-Tyr(PO3H2)-Nbo-NH2 (epimer 2) (SEQ ID NO: 83); trans-4-hydroxy-cinnamoyl-Tyr(PO3H2)-lle-Asn-NH2 (SEQ ID NO: 84); 6-hydroxy-2-naphthoyl-Tyr(Pθ3H2)-He-NH2 (SEQ ID NO: 85); trans-3,4-dihydroxy-cinnamoyl-Tyr(Pθ3H2)-Gln-NH2 (SEQ ID NO: 86); trans-3,4-dihydroxy-cinnamoyl-Tyr(Pθ3H2)-Glu-NH2 (SEQ ID NO: 87); 1-adamantoyl-Tyr(PO3H2)-lle-Asn-NH2 (SEQ ID NO: 93); cyclohexanoyl-Tyr(Pθ3H2)-lle-Asn-NH2 (SEQ ID NO: 94); succinamoyl-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 101); trans-3,4-dihydroxy-cinnamoyl-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 105) (very preferred); trans-3,4-dihydroxy-cinnamoyl-F 2 Pmp-lle-Asn-NH2 (SEQ ID NO: 109) (very preferred); trans-3,4-dihydroxy-cinnamoyl-F 2 Pmp-lle-NH2 (SEQ ID NO: 110); 3-aminobenzyloxycarbonyl-Tyr(PO3H2)-Met-Asn-NH2 (SEQ ID NO: 111); indole-5-ylcarbonyl-L-F2Pmp-lle-Asn-NH2 (SEQ ID NO: 115) (very preferred); 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-Gln-Asn-NH2 (SEQ ID NO: 117) (very preferred); 3-Aminobenzyloxycarbonyl-Tyr(PO3H2)-Ac6C-Asn-NH2 (SEQ ID NO: 120) (very preferred); acetyl-Tyr(PO 3 H 2 )-lle-Asn-NH-(3-naphthalen-1-yl-propyl) (SEQ ID NO: 121 ); acetyl-Tyr(Pθ3H2)-He-Asn-NH-[3-(2-hydroxy-naphthalen-1-yl)-propyl] (SEQ ID NO: 122); acetyl-Tyr(Pθ3H2)-He-Asn-NH-(3-naphthalen-2-yl-propyl) (SEQ-ID-NO: 123); 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-NH-(3-naphthalen-1-yi-propyl) (SEQ ID NO: 140); 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-lle-Asn-NH-[3-(2-hydroxy-naphthalen-1-yl)-propyl] (SEQ ID NO: 141) (very preferred); 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-NH-(3-phenanthren-9-yl-propyl) (SEQ ID NO: 143); 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-NH-(3-methyl-butyl) (SEQ ID NO: 145); and 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-NH-cyclohexyl (SEQ ID NO: 146); or a pharmaceutically acceptable salt thereof if a salt-forming group is present. Most preferred is also indole-5-ylcarbonyI-Tyr-lle-Asn-Gln-NH2 (SEQ ID NO: 112), or a pharmaceutically acceptable salt thereof. The compounds of the present invention can be synthesized according to known procedures, especially by a process comprising reacting a fragment of a compound of formula I, which has a free carboxy group or a reactive derivative thereof, or, in the case of the introduction of X, a free carboxy or sulfo group, or a reactive derivative thereof, with a complementary fragment that has an amino group with at least one free hydrogen atom, or with a reactive derivative thereof, with formation of an amide bond; in the mentioned fragments free functional groups with the exception of those that participate in the reaction if required being present in protected form; and removing any protecting groups present; and, if desired, transforming a compound of formula I into a different compound of formula I; transforming a salt of an obtainable compound of formula I into the free compound or a different salt or an obtainable free compound of formula I into a salt; and/or separating obtainable mixtures of isomers of compounds of formula I into the individual isomers. In the following, more detailed description of the preferred process conditions, X, PTI, -(AA) n -, n and Y have the meanings given for compounds of the formula I, if not mentioned otherwise. Detailed description of preferred reaction conditions The compounds of the present invention preferably can be readily prepared according to well-established, standard liquid or, preferably, solid-phase peptide synthesis methods, general descriptions of which are broadly available (see, for example, in J.M. Stewart and J.D. Young, Solid Phase Peptide Synthesis, 2nd edition, Pierce Chemical Company, Rockford, Illinois (1984), in M. Bodanzsky and A. Bodanzsky, The Practice of Peptide Synthesis, Springer Veriag, New York (1984); and Applied Biosystems 430A Users Manual, ABI Inc., Foster City, California), or they may be prepared in solution, by the liquid phase method or by any combination of solid-phase, liquid phase and solution chemistry, e.g. by first completing the respective peptide portion and then, if desired and appropriate, after removal of any protecting groups being present, by introduction of the residue X by reaction of the respective carbonic or sulfonic acid or a reactive derivative thereof. A fragment with a free carboxy or sulfonic group can be an amino acid (if required, in suitably protected form) or a di- or other appropriate oligopeptide or also (in the case of the introduction of the N-terminal X of compounds of formula I with acylated or sulfonylated terminal amino group) the acylating carbonic or sulfonic acid. A fragment that has an amino group with at least one free hydrogen atom (= a group -NH-) can also be a single amino acid, a di- or other oligopeptide or, in the case of preparation of peptamides (Y = amino or mono- or disubstituted amino), ammonia or mono- or disubstituted ammonia. Reactive derivatives of carbonic or sulfonic acids are preferably reactive esters, reactive anhydrides or reactive cyclic amides. Reactive carbonic acid or reactive sulfonic acid derivatives can also be formed in situ. A reactive derivative of an "amino group with at least one free hydrogen" is preferably derivatized by the reaction with a phosphite, such as diethyl-chlorophosphite, 1 ,2- phenylene-chiorophosphite, ethyl-dichlorophosphite, ethylene-chlorophosphite or tetraethyl- pyrophosphite; or is present in the form of a carbamic acid chloride wherein the amino group participating in the reaction is subtituted by halocarbonyl, such as chiorocarbonyl. Preferably, free amino is used instead of a reactive derivative. The reaction steps required e.g. for the synthesis of amide or sulfonamide bonds usually depend on the type of activation of the carboxylic or sulfo group participating in the reaction. The reactions normally run in the presence of a condensing agent or, when activating the carboxylic or sulfonic acids in the form of anhydrides, of an agent that binds the carboxylic or sulfonic acid formed. In some cases it is also possible to add chaotropic agents such as LiF in N-methylpyrrolidin-2-one. The reactions are especially carried out in a temperature range from -30 to +150 °C, preferably from +10 to +70 °C, and, most preferably, from +20 to +50 °C, if appropriate, in an inert gas atmosphere, e.g. under nitrogen or argon. If desired or appropriate, unreacted amino groups can be acylated after a reaction cycle, e.g. by acetylation of unreacted amino groups with an excess of acetic anhydride/pyri- dine/DMA (1 :1 :8), thus facilitating later purification of the final product. In general, a suitably protected amino acid as a ligand is attached via its carboxyl group (- COOH) to a derivatized, insoluble polymeric support, e.g. a cross-linked polystyrene or polyamide resin, such as a 4-(2',4'-dimethoxyphenyl-[hydroxy- or amino-]methyl)-phenyoxy - polystyrene resin (the polymer is, e.g., a copolymer of styrene with 1% divinylbenzene, 100- 200 mesh) or a PAL-PEG-PS (synonym: PAL-PEG-MBHA-PS) resin (PAL stands for a trisalkoxy, especially trismethoxy, benzylamide linker; PEG for polyethyleneglycol; and MBHA for 4-methylbenzhydrylamine - in this type of resin, polystyrene (PS) supports uniformly incorporate a derivatized polyethylene glycol (PEG) spacer between the functional group on the PS gel bead (e.g. preferred particle size in the range of 75 to 150 μm, crosslinking by 1% divinylbenzene) and the handle or attachment point of the peptide to be synthesized (see J. Org. Chem. 55, 3730 (1990) or in "Peptides: Chemistry and Biology, Proceedings of the Twelfth American Peptide Symposium (Smith, J.A., and Rivier, J.E., eds.) ESCOM, Leiden, The Netherlands (1992), p. 603)) by condensation reactions, or, especially for the synthesis of compounds of formula I with a C-terminal secondary or tertiary amino group Y, said compound being bound to the resin via a carboxy group different from the C-terminal α-carboxy group of an amino acid, e.g. the γ-carboxy group of aspartic acid or the δ-carboxy group of glutamic acid, a 4-(2',4'-dimethoxyphenyl-Fmoc- aminomethyl)-phenoxyacetamido-norleucyl-4-methyl-benzhydrylamine resin (Novabiochem, Laufelfingen, Switzerland). "Suitably protected" refers to the presence of protecting groups on the amino group (e.g. α-NH 2 or β-NH 2 ) and any side-chain functional group (if present) of the amino acid. Di-, tri- or other oligopeptides can be used instead of the amino acids as building blocks (fragments). Synthesis proceeds in a stepwise, cyclical fashion by successively removing the NH 2 protecting group of the amino group to be reacted next and then coupling an activated fragment (e.g. an amino acid, di-, tri- or oligopeptide or the carboxylic acid or sulfonic acid of formula II, X-OH (II) or a reactive derivative thereof, wherein X has the meanings given under formula I) to the deprotected NH 2 (e.g. α- or β-NH 2 ). Preferably, activation of the COOH group of the amino acid to be reacted or ( in the case of the introduction of X) the carboxyl or sulfo group of the acid of of formula II to be attached by the condensation reaction is effected (i) directly with a carbodiimide, e.g. dicydohexylcarbodiimide (DCC), N-ethyl-N'-(3-dimethyl- aminopropyl)-carbodiimide, N,N'-diethylcarbodiimide or N,N'-diisopropylcarbodiimide (DICD); with a carbonyl compound such as carbonyldiimidazole; with 1 ,2-oxazolium compounds such as 2-ethyl-5-phenyl-1 ,2-oxazolium-3'-sulfonate and 2-tert-butyl-5-methylisoxazolium perchlorate; with acylamino compounds such as 2-ethoxy-1 -ethoxycarbonyl- 1 ,2-dihydroqui- noline; with N-[(dimethylamino)-1 H-1 ,2,3-triazolo[4,5-b]pyridin-1-ylmethylene]-N- methylmethanaminium hexafluorophosphate N-oxide (HATU) ; with an uronium compound such as 2-(1 H-benzotriazol-1-yl)-1 ,1 ,3,3-tetramethyluronium tetrafluoroborate (HBTU) or 2-- (pyridon-1-yl)-1 ,1 ,3,3-tetramethyluronium tetrafluoroborate = O-(1,2-dihydro-2-oxo-1 -pyri- dyl)-N,N,N\N'-tetramethyluronium-tetrafluoroborate (TPTU); or phosphonium compounds such as benzotriazol-1-yl-oxy-tris(dimethylamino)-phosphonium hexafluorophosphate (BOP) or benzotriazol-1-yl-oxy-pyrrolidino-phosphonium hexafluorophosphate (PyBOP); (ii) via formation of the symmetric anhydride (obtainable, for example, by condensation of the corresponding acid in the presence of a carbodiimide or 1 -diethylaminopropyne; symmetric anhydrides method), or an asymmetric anhydride, such as the respective carbonic or sulfonic acid bromide, chloride or fluoride (obtainable, for example, by treatment of the respective carbonic or sulfonic acid with thionyl-, phosphopenta- or oxalyl-fluoride, -chloride or -bromide; acid halide (e.g. chloride) method), or (iii) by formation of an "active ester", e.g. an amino- or amido ester, such as a 1 -hydroxy¬ benzotriazole (HOBT) or N-hydroxysuccinimide ester, or an aryl ester, such as a penta- fluorophenyl, 4-nitrophenyl or 2,4,5-tetrachlorophenyl ester (obtainable by treatment of the respective acid with a phenyl with the appropriate substituents, such as 4-nitrophenol or 2,4,5-trichlorophenol, and the like); or by an appropriate combination of any of the reagents and reactions mentioned under (i) to (iii). Useful acid binding agents that can be employed in the condensation reactions are, for example, alkaline metals, carbonates or bicarbonates, such as sodium or potassium carbonate or bicarbonate (if appropriate, together with a sulfate), or organic bases such as sterically hindered organic nitrogen bases, for example tri-lower alkylamines, such as N,N- diisopropyl-N-ethylamine, pyridine or N-methyl-pyrrolidin-2-oπe, which can be used alone or in any appropriate combination. Reactive groups in the monomers of ligands or in the resin-bound or free intermediates resulting from one or more coupling steps can be protected by third groups as protecting groups that are customarily used in peptide synthesis. Examples of protecting groups, their introduction and their removal are, for example, described in standard works such as "Protective groups in Organic Chemistry", Plenum Press, London, New York 1973; "Methoden der organischen Chemie", Houben-Weyl, 4. edition, Vol. 15/1 , Georg-Thieme Veriag, Stuttgart 1974; Th. W. Greene, "Protective Groups in Organic Synthesis", John Wiley & Sons, New York 1981 ; Atherton et al., "Solid Phase Peptide Synthesis - A Practical Approach", IRL Press Oxford University, 1984; Jones, "The Chemical Synthesis of Peptides", Oxford Science Publications, Clavendon Press Oxford, 1991 ; and Bodanszky, "Peptide Chemistry", Springer Veriag Berlin, 1988. The term "protecting groups" comprises also resins used for solid phase synthesis, preferably those specifically mentioned above and below. Examples for hydroxy protecting groups are acyl radicals, such as tert-lower alkoxycarbonyl radicals, for example tert-butoxycarbonyl, etherifying groups, such as tert-lower alkyl groups, for example t-butyl, or silyl- or tin radicals, such as tert-butyl-dimethylsilyl or the tri-n- butyltin radical. Carboxy groups can be protected by groups as defined above for the C-terminal protecting groups Y, preferably by esterifying groups selected from those of the tert-butyl type, from benzyl, from trimethylsilylethyl and from 2-triphenylsilyl groups, or they can be protected as lower alkenyl esters, such as allylic esters. . Amino or guanidino (e.g. in H-Arg-OH) groups can be protected by removable acyl groups or by arylmethyl, etherified mercapto, 2-acyl-lower alk-1 -enyl, a silyl group or an organic sulfonyl group or tin amino protecting groups; tert-butoxycarbonyl, allyloxycarbonyl, benzyl¬ oxycarbonyl, 4-nitrobenzyloxycarbonyl, 2-chlorobenzyloxycarbonyl, 2-bromobenzyloxy- carbonyl, diphenylmethoxycarbonyl, nitrophenylsulfenyl, 2,2,2-trichloroethoxycarbonyl, 2,2,5,7,8-pentamethylchroman-6-sulfonyl (PMC - very preferred), 2,2,4,6,7-pentamethyl- dihydrobenzofuran-5-sulfonyl (Pbf) or 4-methoxy-2,3,6-trimethylbenzenesuifonyl (Mtr) being especially preferred. Carbamide groups (for example, in the side chains of asparagine and glutamine) can be protected at the nitrogen atom by arylmethyl groups, preferably triphenylmethyl (trityl) or analogues thereof with one or more lower alkoxy, such as methoxy, and/or lower alkyl, such as methyl, substituents in one or more phenyl rings. Phosphono groups can be protected in the form of diesters, e.g. in the form of di-lower alkyl esters, e.g. as diethylphosphonate (-P(=O)(OC 2 H 5 ) 2 ) or di-tert-butylphosphonate. Imino groups (e.g. in imidazole) can be protected by 2,4-dinitrophenyl, trityl, tert-butoxy¬ carbonyl or p-toluenesulfonyl, or (e.g. in indole) by formyl or tert-butoxycarbonyl. Mercapto groups can be protected, e.g., by acetamidomethyl, by trityl or by p-methylbenzyl. A large number of methods of removing protective groups in the final products or any inter¬ mediates are known in the art and comprise, inter alia, β-elimination, solvolysis, hydrolysis, alcoholysis, acidolysis, photolysis, enzymatical removal, treatment with a base or reduction. The protective groups are usually removed after the complete synthesis of the resin-bound molecule by conventional methods of peptide chemistry, conveniently by treatment with 95 % trifluoroacetic acid (Fmoc-chemistry). In some cases, strong nucleophiles, such as dimethyl sulfide and/or 2-ethanedithiol, may be additionally added to capture the generated compounds resulting from the protecting groups, e.g. in a combination such as trimethyl- silyltrifluoro-methansulfonate/dimethyisulfide/trifluoroacetic acid/ethanedithiol/m-cresol. Cleavage of phosphonate diester protecting groups is possible in appropriate solvents, such as acetonitrile, in the presence of tri-lower alkylsilylhalogenides, such as trimethylsilyl- iodide, and subsequent hydrolysis of the resulting tri-lower alkylsilyl-ester intermediate in the presence of an acid, especially a lower alkanoic acid, such as acetic acid, in aqueous solution. Cleavage of lower-alkenoic esters of carboxy groups, such as allyloxycarbonyl, is preferably effected in a solution of a lower alkanoic acid, such as acetic acid, and a sterically hindered base, such as N-methylmorpholine, in an appropriate solvent, such as a halogenated hydrocarbon, especially chloroform, in the presence of tetrakis- (triphenylphosphin)palladium, preferably under inert gas, such as argon. The two preferred methods of solid phase peptide synthesis are the Boc and the Fmoc methods, which are named with reference to their use of the tert-butoxycarbonyl (Boc) or 9- fluorenylmethyloxycarbonyl (Fmoc) group, respectively, to protect the α-NH 2 or α-NHR 3 of the amino acid residue to be coupled (see J. M. Stewart, J. D. Young, Solid-Phase Peptide Synthesis, 2n edn., Pierce, Rockford, Illinois (1984) or G. Barany, R.B. Merrifield, Solid- phase Peptide Synthesis, in: The Peptides, Vol. 2 (E. Gross, J. Meienhofer, eds.), Academic Press, New York (1979)); and E. Atherton and R.C. Sheppard, in Solid-Phase Peptide Synthesis-A Practical Approach, ed. D. Rickwood and B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989), respectively). In the more established Boc method, the acid-lability of the Boc group is exploited and trifluoroacetic acid (TFA) treatment is used in order to remove the protective group. Preferred third groups as protecting groups (for functional groups in side chains) are relatively stable in weak acid, e.g. TFA. Most can be cleaved by strong acids such as hydrofluric acid (HF) or trifluoromethanesulfonic acid. A small number of side chain groups (e.g. 2,4-dinitrophenyl protected imino in the histidyl side chain) may require a separate deprotection step, e.g. treatment with thiophenol or ammonolysis. After synthesis, the product is typically cleaved from the resin and simultaneously deprotected by HF treatment at low temperature (e.g. around 0 °C). The Fmoc-group can be cleaved off preferably in the presence of a mild nitrogen base, preferably piperidine, in an inert solvent, preferably dimethyl acetamide, thereby allowing the use of side-chain protecting groups which are labile to milder treatment, e.g. TFA. Preferably, an acid labile ether resin such as HMP-resin (p-hydroxymethylphenoxymethyl polystyrene), 4-(2',4'-dimethoxyphenyl-hydroxymethyl)-phenoxy-polystyrene (Rink-resin), or a resin with a benzyloxy- or alkyloxy linker (see Wang, J. Amer. Chem. Soc. 95, 1328 (1973); or, for the synthesis of compounds with a C-terminal amino group X (forming a car¬ boxamide) which are preferred, 4-(2',4'-dimethoxyphenyl-aminomethyl)-phenoxypolysty- rene or -phenoxymethyl-polystyrene (Rink et al., Tetrahedron. Lett. 28(33), 3787-90 (1987); Novabiochem, Laufelfingen, Switzerland); or a PAL-PEG-PS resin (Millipore, Bedford, USA) is used as the solid support, permitting simultaneous cleavage/deprotection in TFA. Additional process steps Compounds of formula I can be transformed into different compounds of formula I, e.g. by oxydation and hydrolysis. For the preferred oxidation of mercapto groups, e.g. lower alkyl-mercapto groups, such as methylthio, which are preferably oxidised to the respective sulfinyl groups, e.g. lower alkyl sulfinyl, such as methylsulfinyl, organic or preferably inorganic peroxides, such as hydrogen peroxide, can be employed. For example, reaction of lower alkylthio compounds with hydrogen peroxide in concentrations from 2 to 30 volume-% at preferred temperatures from 0 to 50 °C, especially around room temperature, leads to the respective lower alkyl sulfinyl compounds. For the preferred hydrolysis of esterified carboxy groups, such as lower alkoxycarbonyl groups, well-known conditions for hydrolysis are used, for example hydrolysis in the presence of a base, e.g. a hydroxide of an alkaline metal, such as sodium hydroxide, under conditions known in the art, e.g. in an aqueous solvent at preferred temperatures between 0 and 50 °C, preferably at room temperature. Salts of compounds of formula I having at least one salt-forming group may be prepared in a manner known per se. For example, salts of compounds of formula I having acid groups may be formed, for example, by treating the compounds with metal compounds, such as alkali metal salts of suitable organic carboxylic acids, e.g. the sodium salt of 2-ethylhexanoic acid, with organic alkali metal or alkaline earth metal compounds, such as the corres¬ ponding hydroxides, carbonates or hydrogen carbonates, such as sodium or potassium hydroxide, carbonate or hydrogen carbonate, with corresponding calcium compounds or with ammonia or a suitable organic amine, stoichiometric amounts or only a small excess of the salt-forming agent preferably being used. Acid addition salts of compounds of formula I are obtained in customary manner, e.g. by treating the compounds with an acid or a suitable anion exchange reagent. Internal salts of compounds of formula I containing acid and basic salt-forming groups, e.g. a free carboxy group and a free amino group, may be formed, e.g. by the neutralisation of salts, such as acid addition salts, to the isoelectric point, e.g. with weak bases, or by treatment with ion exchangers. Salts can be converted in customary manner into the free compounds; metal and ammonium salts can be converted, for example, by treatment with suitable acids, and acid addition salts, for example, by treatment with a suitable basic agent. Mixtures of isomers obtainable according to the invention can be separated in a manner known per se into the individual isomers; diastereoisomers and/or cis/trans-isomers can be separated, for example, by partitioning between poiyphasic solvent mixtures, recrystal¬ lisation and/or chromatographic separation, for example over silica gel or by e.g. medium pressure liquid chromatography over a reversed phase column, and racemates can be separated, for example, by the formation of salts with optically pure salt-forming reagents and separation of the mixture of diastereoisomers so obtainable, for example by means of fractional crystallisation, or by chromatography over optically active column materials. Starting materials: The present invention relates also to novel starting materials and/or intermediates and to processes for their preparation. The starting materials used and the reaction conditions selected are preferably those that result in the compounds described as being preferred. Unless a specific method of synthesis is indicated for starting materials, the starting materials are known, can be prepared according to processes known per se, especially in analogy to methods given in the Examples, and/or are commercially available. For example, suitably protected and/or preactivated D-, (D,L)- or L- amino acids, unnatural amino acids, di-, tri- or oligopeptides, derivatized and/or preloaded resins, the ancillary reagents and solvents required for either Boc or Fmoc peptide synthesis are commercially available from various suppliers or can be prepared readily according to standard procedures. In addition, di- or other oligopeptoids can be prepared readily according to standard procedures. In addition, automated peptide synthesizers with optimized, preprogrammed Boc and Fmoc synthesis cycles are available from numerous sources. The starting materials for the phosphotyrosine mimics and the respective protected derivatives can be synthesized according to methods known in the art; (e.g., for phosphono¬ methyl-phenylalanine, especially 4-phosphonomethyl-phenylalanine, see Synthesis 1991. 1019, Tetrahedron Lett. 32(43), 6061 (1991), Tetrahedron Lett. 33(9), 1193 (1992) and SynLett 1994, 233-254; for phosphono-(α-fluoro)methyl-phenylalanine, especially 4-phos- phono-(α-fluoro)methyl-phenylalanine, see J. Chem. Soc, Perkin Trans. 1, 1986(1), 913-917 or Cancer Cells 2, 95 (1990) and J. Org. Chem 58, 1336-1340 (1993), for phosphono-(α,α- difiuoro)methyl-phenylalanine, especially 4-phosphono-(α,α-difluoro)methyl-phenyialanine, see Tetrahedron Lett. 35, 551-554 (1994), Tetrahedron Lett. 34(22), 3543 (1993) and Tetrahedron Lett. 33(29), 4137 (1992), for phosphono-(α-hydroxy)methyl-phenylalanine, especially 4-phosphono-(α-hydroxy)methyl-phenylalanine, see Drugs of the Future 17, 119 (1992) and J. Org. Chem. 58, 1336-1340 (1993), for O-sulfo-tyrosine, such as 4-(O-sulfo)- tyrosine (= tyrosine sulfate), see Chem. Pharm. Bull. 41, 376-380 (1993), for dicarboxy- methoxy-phenylalanine (= (HOOC) 2 -CH 2 -O-phenylalanine, especially 4-(dicarboxymethoxy)- phenylalanine, see Abstract No. 014.024.114 presented at the 109 th American Chemical Society Meetin, April 2-6 (1995) in Anaheim, California; and for phosphono-phenylalanine, such as 4-phosphonophenylalanine, see Tetrahedron 46, 7793-7802 (1990)). General process conditions The following applies in general to all processes mentioned hereinbefore and hereinafter, while reaction conditions specifically mentioned above or below are preferred: Functional groups in starting materials the reaction of which is to be avoided, especially carboxy, amino, hydroxy, mercapto and sulfo groups, can be protected by suitable protect¬ ing groups (conventional protecting groups) which are customarily used in the synthesis of peptide compounds, and also in the synthesis of cephalosporins and penicillins as well as nucleic acid derivatives and sugars. These protecting groups may already be present in the precursors and are intended to protect the functional groups in question against undesired secondary reactions, such as acylation, etherification, esterification, oxidation, solvolysis, etc. In certain cases the protecting groups can additionally cause the reactions to proceed selectively, for example stereoselectively. It is characteristic of protecting groups that they can be removed easily, i.e. without undesired secondary reactions taking place, for example by solvolysis, reduction, photolysis, and also enzymatically, for example also under physio¬ logical conditions, and, especially, that they are not present in the end products. The protection of functional groups by such protecting groups, the protecting groups them¬ selves and the reactions for their removal are described, for example, in standard works such as J. F. W. McOmie, "Protective Groups in Organic Chemistry", Plenum Press, London and New York 1973, in Th. W. Greene, "Protective Groups in Organic Synthesis", Wiley, New York 1981 , in "The Peptides", Volume 3 (E. Gross and J. Meienhofer, eds.), Academic Press, London and New York 1981 , in "Methoden der organischen Chemie", Houben-Weyl, 4th edition, Volume 15/1, Georg Thieme Veriag, Stuttgart 1974, in H.-D. Jakubke and H. Jescheit, "Aminosauren, Peptide, Proteine" ("Amino acids, peptides, proteins"), Veriag Chemie, Weinheim, Deerfield Beach and Basle 1982, and in Jochen Lehmann, "Chemie der Kohlenhydrate: Monosaccharide und Derivate" ("The Chemistry of Carbohydrates: monosaccharides and derivatives"), Georg Thieme Veriag, Stuttgart 1974. When several protected functional groups are present, if desired the protecting groups can be so selected that more than one such group can be removed simultaneously, for example by acidolysis, such as by treatment with trifluoroacetic acid, or with hydrogen and a hydrogenation catalyst, such as a palladium-on-carbon catalyst. Conversely, the groups can also be so selected that they cannot all be removed simultaneously, but rather in a desired sequence, the corresponding intermediates being obtained. In view of the close relationship between the compounds of formula I and their salts and starting materials (starting materials and intermediates) in free form and in the form of their salts, any reference hereinbefore and hereinafter to a free compound or a salt thereof is to be understood as meaning also the corresponding salt or free compound, respectively, where appropriate and expedient. All the above-mentioned process steps can be carried out under reaction conditions that are known per se, preferably those mentioned specifically, in the absence or, customarily, in the presence of solvents or diluents, preferably solvents or diluents that are inert towards the reagents used and dissolve them, in the absence or presence of catalysts, condensation agents or neutralising agents, for example ion exchangers, such as cation exchangers, e.g. in the H + form, depending on the nature of the reaction and/or of the reactants at reduced, normal or elevated temperature, for example in a temperature range of from approximately - 100°C to approximately 190°C, preferably from approximately -80°C to approximately 150°C, for example at from -80 to -60°C, at room temperature, at from -20 to 40°C or at reflux temperature, under atmospheric pressure or in a closed vessel, where appropriate under pressure, and/or in an inert atmosphere, for example under an argon or nitrogen atmosphere. At all stages of the reactions, mixtures of isomers that are formed can be separated into the individual isomers, for example diastereoisomers or enantiomers, or into any desired mix- tures of isomers, for example racemates or mixtures of diastereoisomers, for example ana¬ logously to the methods described under "Additional process steps". The solvents from which those solvents that are suitable for any particular reaction may be selected include, for example, water, esters, such as lower alkyl-lower alkanoates, for example ethyl acetate, ethers, such as aliphatic ethers, for example diethyl ether, or cyclic ethers, for example tetrahydrofuran, liquid aromatic hydrocarbons, such as benzene or toluene, alcohols, such as methanol, ethanol or 1- or 2-propanol, nitriles, such as aceto¬ nitrile, halogenated hydrocarbons, such as methylene chloride, acid amides, such as dimethylformamide, bases, such as heterocyclic nitrogen bases, for example pyridine, carboxylic acid anhydrides, such as lower alkanoic acid anhydrides, for example acetic anhydride, cyclic, linear or branched hydrocarbons, such as cydohexane, hexane or iso¬ pentane, or mixtures of those solvents, for example aqueous solutions, unless otherwise indicated in the description of the processes. Such solvent mixtures may also be used in working up, for example by chromatography or partitioning. The compounds, including their salts, may also be obtained in the form of hydrates, or their crystals may, for example, include the solvent used for crystallisation. Different crystalline forms may be present. If necessary, protected starting materials may be used in all process steps and the protecting groups may be removed at suitable stages of the reaction. The invention relates also to those forms of the process in which a compound obtainable as intermediate at any stage of the process is used as starting material and the remaining process steps are carried out, or in which a starting material is formed under the reaction conditions or is used in the form of a derivative, for example in protected form or in the form of a salt, or a compound obtainable by the process according to the invention is produced under the process conditions and processed further in sjtu. In the process of the present invention there are preferably used those starting materials which result in the compounds of formula I described at the beginning as being especially valuable. Special preference is given to reaction conditions that are analogous to those mentioned in the Examples. Pharmaceutical Compositions: The invention relates also to pharmaceutical compositions comprising compounds of formula I, to their use in the therapeutic (including prophylactic) treatment of the diseases mentioned above, to the compounds for said use and to the preparation of pharmaceutical preparations. The pharmacologically acceptable compounds of the present invention may be used, for example, for the preparation of pharmaceutical compositions that comprise an effective amount of the active ingredient together or in admixture with a significant amount of inorganic or organic, solid or liquid, pharmaceutically acceptable carriers. The invention relates also to a pharmaceutical composition that is suitable for administration to a warm-blooded animal, especially a human (or to cells or cell lines derived from a warm¬ blooded animal, especially a human, e.g. lymphocytes), for the treatment or preven-tion of (= prophylaxis against) a disease that responds to diseases that respond to inhibition of the interaction of proteins comprising SH2 domains and phosphoproteins, especially a phosphorylated protein tyrosine kinase or modified versions thereof, preferably inhibition of the interaction of Grb2 SH2 with a phosphoprotein containing a -Tyr(PO 3 H 2 )-X-Asn- motif, such as phosphorylated EGFR protein tyrosine kinase or modified derivatives thereof, but also other phospho-proteins such as SHC or modified derivatives thereof, comprising an amount of a corn-pound of formula I or a pharmaceutically acceptable salt thereof, which is effective for said inhibi-tion, especially the inhibition of the interaction of Grb2 SH2 with with a phosphoprotein con-taining a -Tyr(PO 3 H 2 )-X-Asn- motif, such as phosphorylated EGFR protein tyrosine kinase or modified derivatives thereof, but also other phospho-proteins such as SHC, or truncated derivatives thereof, together with at least one pharmaceutically acceptable carrier. The pharmaceutical compositions according to the invention are those for enteral, such as nasal, rectal or oral, or parenteral, such as intramuscular or intravenous, administration to warm-blooded animals (humans and animals), that comprise an effective dose of the pharmacologically active ingredient, alone or together with a significant amount of a pharmaceutically acceptable carrier. The dose of the active ingredient depends on the species of warm-blooded animal, the body weight, the age and the individual condition, individual pharmacokinetic data, the disease to be treated and the mode of administration. The invention relates also to a method of treating diseases that respond to inhibition of the interaction of proteins comprising SH2 domains and phosphoproteins, especially the phos¬ phorylated protein tyrosine kinases or modified versions thereof; preferably of Grb2 SH2 with a phospho-protein containing a -Tyr(PO 3 H 2 )-X-Asn- motif, such as phosphorylated EGFR protein tyrosine kinase or modified derivatives thereof, but also other phospho¬ proteins such as SHC or modified derivatives thereof; which comprises administering a prophylactically or especially therapeutically effective amount of a compound of formula I according to the invention, especially to a warm-blooded animal, for example a human, that, on account of one of the mentioned diseases, requires such treatment. The dose to be administered to warm-blooded animals, for example humans of approximately 70 kg body weight, is from approximately 3 mg to approximately 30 g, preferably from approximately 10 mg to approximately 1.5 g, for example approximately from 100 mg to 1000 mg per person per day, divided preferably into 1 to 3 single doses which may, for example, be of the same size. Usually, children receive half of the adult dose. The pharmaceutical compositions comprise from approximately 1 % to approximately 95%, preferably from approximately 20 % to approximately 90%, active ingredient. Pharma¬ ceutical compositions according to the invention may be, for example, in unit dose form, such as in the form of ampoules, vials, suppositories, dragees, tablets or capsules. The pharmaceutical compositions of the present invention are prepared in a manner known perse, for example by means of conventional dissolving, lyophilising, mixing, granulating or confectioning processes. Solutions of the active ingredient, and also suspensions, and especially isotonic aqueous solutions or suspensions, are preferably used, it being possible, for example in the case of lyophilised compositions that comprise the active ingredient alone or together with a carrier, for example mannitol, for such solutions or suspensions to be produced prior to use. The pharmaceutical compositions may be sterilised and/or may comprise excipients, for example preservatives, stabilisers, wetting and/or emulsifying agents, solubilisers, salts for regulating the osmotic pressure and/or buffers, and are prepared in a manner known perse, for example by means of conventional dissolving or lyophiiising processes. The said solutions or suspensions may comprise viscosity-increasing substances, such as sodium carboxy¬ methylcellulose, carboxymethylcellulose, dextran, polyvinylpyrrolidone or gelatin. Suspensions in oil comprise as the oil component the vegetable, synthetic or semi-synthetic oils customary for injection purposes. There may be mentioned as such especially liquid fatty acid esters that contain as the acid component a long-chained fatty acid having from 8 to 22, especially from 12 to 22, carbon atoms, for example lauric acid, tridecylic acid, myristic acid, pentadecylic acid, palmitic acid, margaric acid, stearic acid, arachidic acid, behenic acid or corresponding unsaturated acids, for example oleic acid, elaidic acid, erucic acid, brasidic acid or linoleic acid, if desired with the addition of antioxidants, for example vitamin E, β-carotene or 3,5-di-tert-butyl-4-hydroxytoluene. The alcohol component of those fatty acid esters has a maximum of 6 carbon atoms and is a mono- or poly-hydroxy, for example a mono-, di- or tri-hydroxy, alcohol, for example methanol, ethanol, propanol, butanol or pentanol or the isomers thereof, but especially glycol and glycerol. The following examples of fatty acid esters are therefore to be mentioned: ethyl oleate, isopropyl myristate, isopropyl palmitate, "Labrafil M 2375" (polyoxyethylene glycerol trioleate, Gattefosse, Paris), "Miglyol 812" (triglyceride of saturated fatty acids with a chain length of C 8 to Cι 2 , Huls AG, Germany), but especially vegetable oils, such as cottonseed oil, almond oil, olive oil, castor oil, sesame oil, soybean oil and more especially groundnut oil. The injection compositions are prepared in customary manner under sterile conditions; the same applies also to introducing the compositions into ampoules or vials and sealing the containers. Pharmaceutical compositions for oral administration can be obtained by combining the active ingredient with solid carriers, if desired granulating a resulting mixture, and process¬ ing the mixture, if desired or necessary, after the addition of appropriate excipients, into tablets, dragee cores or capsules. It is also possible for them to be incorporated into plastics carriers that allow the active ingredients to diffuse or be released in measured amounts. Suitable carriers are especially fillers, such as sugars, for example lactose, saccharose, mannitol or sorbitol, cellulose preparations and/or calcium phosphates, for example tricalcium phosphate or calcium hydrogen phosphate, and binders, such as starch pastes using for example corn, wheat, rice or potato starch, gelatin, tragacanth, methylcellulose, hydroxypropylmethylcellulose, sodium carboxymethylcellulose and/or polyvinylpyrrolidone, and/or, if desired, disintegrators, such as the above-mentioned starches, also carboxy¬ methyl starch, crosslinked polyvinylpyrrolidone, agar, alginic acid or a salt thereof, such as sodium alginate. Excipients are especially flow conditioners and lubricants, for example silicic acid, talc, stearic acid or salts thereof, such as magnesium or calcium stearate, and/or polyethylene glycol. Dragee cores are provided with suitable, optionally enteric, coatings, there being used, inter alia, concentrated sugar solutions which may comprise gum arabic, talc, polyvinylpyrrolidone, polyethylene glycol and/or titanium dioxide, or coating solutions in suitable organic solvents, or, for the preparation of enteric coatings, solutions of suitable cellulose preparations, such as ethylcellulose phthalate or hydroxypropylmethylcellulose phthalate. Capsules are dry-filled capsules made of gelatin and soft sealed capsules made of gelatin and a plasticiser, such as glycerol or sorbitol. The dry-filled capsules may comprise the active ingredient in the form of granules, for example with fillers, such as lactose, binders, such as starches, and/or glidants, such as talc or magnesium stearate, and if desired with stabilisers. In soft capsules the active ingredient is preferably dissolved or suspended in suitable oily excipients, such as fatty oils, paraffin oil or liquid polyethylene glycols, it being possible also for stabilisers and/or antibacterial agents to be added. Dyes or pigments may be added to the tablets or dragee coatings or the capsule casings, for example for identification purposes or to indicate different doses of active ingredient. Examples: Embodiments of the invention are described in the following specific examples which are not to be construed to be intended to limit the scope of the invention in any way, but serve merely for illustration: Temperatures, if not mentioned: room temperature/ambient temperature. In mixtures, relations of parts of solvent or eluent or reagent mixtures in liquid form are given as volume relations (v/v), if not indicated otherwise. Symbols used for amino acids and peptides are in accordance with IUPAC-IUB Commission on Biochemical Nomenclature. If not mentioned otherwise, amino acids are present in the L- form. Other abbreviations used are: Abbreviations: Acsc: bivalent radical of 1-aminocyclopentane carboxylic acid (Aldrich, Buchs, Switzerland); Acβc: bivalent radical of 1 -aminocyclo-hexane carboxylic acid (Fluka, Buchs, Switzerland); Ac 7 c = bivalent radical of 1-aminocyclopentane carboxylic acid (see N. Zelinsky and G. Stadnikoff, Chem. Ber., 39, 1722-1732, (1906)); βAla: beta Alanyl = bivalent radical of 3 aminopropionic acid; Boc: tert-Butoxycarbonyl; BOP: benzotriazole- 1-yl- oxy-tris-(dimethylamino)-phosphoniumhexa-fluorophosphate; DHph = bivalent radical of D- homophenylalanine (Bachem, Bubendorf, Switzerland) ;Fmoc: fluorenylmethoxy-carbonyl; Fmoc-PAL-PEG-PS (Millipore, Bedford, USA): a resin used for peptide synthesis; F2Pmp: 4-phosphono(difluoromethyl)-L-phenyl-alanine; HATU = N-[(dimethylamino)-1 H-1 ,2,3- triazolo[4,5-b]pyridin-1-ylmethylene]-N-methylmethanaminiumhexafluorophosphate N-oxide; HBTU: 2-(1 H-benzotriazol-1-yl)-1 ,1 ,3,3-tetramethyluronium tetrafluoroborate; HOBt: N- hydroxy-benzotriazole; Hph = bivalent radical of L-homophenylalanine (Bachem, Bubendorf, Switzerland); HPLC: high performance liquid chromatography; HPLC System A is defined in Example 1 ; HPLC System B is defined in Example 45; HPLC System C is defined in Example 51 ; HPLC system D is defined in Example 123; MeCN = acetonitrile; Nbo = bivalent radical of 2-amino-norbornane carboxylic acid (Aldrich, Buchs, Switzerland); PAL: tris-alkyl- (= methyl-)-oxybenzylamide linker; PEG: polyethylene glycol; Pmp = bivalent radical of p-phosphonomethyl-phenylalanine (see Example 121); R f : ratio of fronts in thin layer chromatography employing silica gel plates (Merck, Darmstadt, FRG); TFA = trifluoroacetic acid; Tie = bivalent radical of L-α-t-butyl-glycine (= tert-leucine; see Example 120); .R: retention time in HPLC; Tyr(PO 3 H2): [p-(O-Phosphono)-Tyr]. Example 1 : 3-Aminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 1) The peptide is synthesized manually on a 4-(2',4'-dimethoxyphenyl-aminomethyl)-phenoxy- resin (Fmoc-protected at the amino group, obtainable from Novabiochem, Laufelfingen, Switzerland; 0.47 mmol/g, 300 mg), employing the fluorenylmethoxycarbonyl (Fmoc) strategy (see E. Atherton and R.C. Sheppard, in Solid-Phase Peptide Synthesis-A Practical Approach, ed. D. Rickwood and B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989). Fmoc is removed with piperidine/dimethylacetamide (1 :4, v/v; 6 x 2 min), followed by washing with methanol (3 x 1 min), Λ/-methylpyrrolidin-2-one (2 x 1 min), methanol (3 x 1 min), and Λ/-methylpyrrolidin-2-one (3 x 2 min). Coupling is achieved by first dissolving the Fmoc-amino acid (2 equiv.), diisopropylethylamine (2.2 equiv.), and the 2-(2-pyridon-1-yl)- 1 ,1 ,3,3-tetramethyluroniumtetrafluoroborate reagent (TPTU, Senn Chemicals, Dielsdorf, Switzerland; 2 equiv.) in Λ/-methylpyrrolidin-2-one, then waiting 3 min for preactivation, adding the mixture to the resin, and finally shaking for at least 45 min. The side chain of asparagine and glutamine is protected with the trityl group. The incorporation of N α -Fmoc- Tyr(PO3H2)-OH (see Biochemistry 32, 4354 (1993)) (3 equiv.) is accomplished with benzotriazole-1-yl-oxy-tris-(dimethylamino)-phosphoniumhexafluorophosphate/N- hydroxybenzotriazole (1 :1 ; 3 equiv.; first coupling) in the presence of diisopropylethylamine (7 equiv.) and N-[(dimethylamino)-1 H-1 ,2,3-triazolo[4,5-b]pyridin-1-ylmethylene]-N- methylmethanaminium hexafluorophosphate N-oxide (3 equiv., second coupling) in the presence of diisopropylethylamine (7 equiv.). 3-N-terf-butoxy-carbonyl-aminobenzyl-4- nitrophenyi-carbonate (3 equiv.) is coupled to the Λ/-terminal residue of the peptide resin in the presence of an equimolar amount of diisopropylethyl-amine in N-methylpyrrolidin-2-one during 17 h at room temperature. The complete peptide resin obtained after the final coupling reaction is simultaneously deprotected and cleaved by treatment with trifluoroacetic acid/H2θ (95:5, v/v) for 3 h at room temperature. The filtrate from the cleavage reaction is precipitated in diisopropyl ether-petroleum ether (1 :1 , v/v, 0 °C), and the precipitate is collected by filtration. The crude peptide is purified by medium-pressure liquid chromatography using a C- | 8-column eluted with an acetonitrile-water gradient containing 0.1 % of TFA (Merck ® LICHROPREP RP-18, 15-25 urn bead diameter, reversed phase HPLC column material based on C 18 -derivatized silicagel, Merck, Darmstadt, FRG; column length 46 cm, diameter 3.6 cm; flow rate 53.3 ml/min; detection at 215 nm). The title compound is obtained: Mass spectral analysis (matrix-assisted laser-desoption ionization time-of-flight mass spectrometry, MALDI-TOF) reveales a molecular mass within 0.1 % of the expected values (negative-ion mode): 763.7 (calc. 763.7, C32H44NsOi2Pi)- The purity of the peptide is verified by reversed-phase analytical HPLC on a Nucleosil Cis-column (250 x 4 mm, 5 μm, 100 A): linear gradient over 10 min of MeCN/0.09% TFA and H2θ/0.1%TFA from 1 :49 to 3:2; flow rate 2.0 ml/min, detection at 215 nm; single peak at tR= 5.22 min (HPLC System A). The starting materials are prepared as follows: a) 3-N-tert-Butoxycarbonyl-aminobenzyl alcohol B0C2O (13.4 ml, 60 mmol) is added to a solution of 3-aminobenzyl alcohol (2.46 g, 20 mmol; Aldrich, Buchs, Switzerland) in 0.5 N NaOH (25 ml) and stirring is continued until completion of the reaction. The alkaline solution is extracted with petroleum ether (2x10 ml); the ether extracts are discarded. The aqueous phase is acidified with a 5% solution of citric acid to pH 2-3 and extracted with ethyl acetate (2x30 ml). The ethyl acetate extracts are pooled, washed with water (2x30 ml), dried over anhydrous Na2SO4 and evaporated in vacuo. Rf= 0.72 (chloroform:methanol:water:acetic acid = 750:270:50:5, v/v/v/v). b) 3-N-fe- -Butoxycarbonyl-aminobenzyl-4-nitrophenyl-carbonate A solution of 3-N-teιt-butoxycarbonyl-aminobenzyl alcohol (1.0 g) in anhydrous pyridine (18 ml) is cooled in an ice-water bath and 4-nitrophenyl chloroformate is added with stirring. The solution is stirred for 17 h at room temperature and then added to a mixture of diisopropyl ether/petroleum ether (1 :1 , v/v; 200 ml). The ether mixture is extracted with brine (1x50 ml) and then with water (7x 50 ml), dried over anhydrous Na2SO4 and evaporated in vacuo. The crude compound is purified by flash chromatography on silica gel, using dichloromethane as eluent. Rf= 0.66 (chloroform/methanol = 95:5, v/v). The following examples are obtained in analogy to the title compound of Example 1 : Example 2: 2-Aminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 2) Title compound: Mass spectral analysis (negative-ion mode): 763.3 (calc. 763.7, c 32 H 44 N 8°12 p l)' *R= 5 - 50 min (HPLC System A). The starting material is obtained as follows: a) 2-N-tert-Butoxycarbonyl-aminobenzyl-4-nitrophenyl-carbonate The title compound is synthesized as described for 3-N-tetf-butoxycarbonyl-aminobenzyl-4- nitrophenyl-carbonate (Examples 1 a) and b)). Rf= 0.92 (dichloromethane:methanol:wa- teπacetic acid = 850:130:15:5, v/v/v/v), starting from 2-aminobenzyl alcohol (Aldrich, Buchs, Switzerland). Example 3: 3-Aminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-NH2 (TFA salt) (SEQ ID NO: 3) Title compound: Mass spectral analysis (negative-ion mode): 635.7 (calc. 635.6, C 27 H 36 N 6°10 P 1). R= 5.54 min (HPLC System A). Example 4:1 -(3-Aminophenyl)ethyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 4), Diastereomer A: Title compound: Mass spectral analysis (negative-ion mode): 777.8 (calc. 777.8, C 33 H 46 N 8°12 P 1). *R= 5 - 41 min (HPLC System A). The starting material is obtained as follows: a) 1-(3-N-tert-Butoxycarbonyl-aminophenyl)ethyl-4-nitrophenyl-carbonate The title compound is synthesized as described for 3-N-tert-butoxycarbonyl-aminobenzyl-4- nitrophenyl-carbonate (Example 1 b)), starting from 1 -(3-aminophenyl)ethanol (Aldrich, Buchs, Switzerland). Rf= 0.54 (chloroform:methanol:water:acetic acid = 900:100:10:5, v/v/v/v). Example 5: 1-(3-Aminophenyl)ethyloxycarbonyl-Tyr(PO3H 2 )-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 5) Diastereomer B: Title compound: Mass spectral analysis (negative-ion mode): 777.2 (calc. 777.8, C 33 H 46 N 8°12 P 1). *R= 5 - 61 min(HPLC System A). Exajτιp!e_6 _3-Aminobenzyloxycarbonyl-Tyr(Pθ3H2)-Ac5C-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 6) Title compound: Mass spectral analysis (negative-ion mode): 761.7 (calc. 761.7, C 32 H 42 N 8°12 P 1). *R= 4 - 28 min (HPLC System A). The starting material is obtained as follows: a) Fmoc-L-amino-1 -cvclopentanecarboxylic acid The title compound is synthesized starting from 1 -amino-1-cyclopentanecarboxylic acid (Aldrich, Buchs, Switzerland) according to a procedure known in the art (see E. Atherton et al., in: Solid-Phase Peptide Synthesis - A Practical Approach; D. Rickwood an B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989): R f = 0.79 (chloro- form:methanol:water:acetic acid 750:270:50:5, v/v/v/v). Example 7: 3-Aminobenzyloxycarbonyl-Tyr(Pθ3H2)-Ac6C-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 7) Title compound: Mass spectral analysis (negative-ion mode): 775.6 (calc. 775.7, C 33 H 44 N 8°12 P 1). *R= 5 - 33 min (HPLC System A). The starting material is prepared as follows: a) Fmoc-L-amino-1 -cvclohexanecarboxylic acid The title compound is synthesized starting from 1-amino-1-cyclohexanecarboxylic acid (Janssen, Olen, Belgium) according to a procedure known in the art (see E. Atherton et al., in: Solid-Phase Peptide Synthesis - A Practical Approach; D. Rickwood an B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989): R = 0.84 (chloro-form:methanol:wa- teπacetic acid 750:270:50:5, v/v/v/v). a) Fmoc-L-amino-1 -cvclopentanecarboxylic acid The title compound is synthesized starting from 1 -amino-1 -cyclopentanecarboxylic acid (Aldrich, Buchs, Switzerland) according to a procedure known in the art (see E. Atherton et al., in: Solid-Phase Peptide Synthesis - A Practical Approach; D. Rickwood an B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989): R f = 0.79 (chloro- form:methynol:water:acetic acid 750:270:50:5, v/v/v/v). Examp!e_8 _2-(4-Methyl-5-thiazolyl)-ethyloxycarbonyl-Tyr(PO3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 8) Title compound: Mass spectral analysis (negative-ion mode): 783.7 (calc. 783.8, C3i H 44 N 8 Oi2PιSι), t R = 5.09 min(HPLC System A). The starting material is obtained as follows: a) 2-(4-Methyl-5-thiazole)-ethyl-4-nitrophenyl-carbonate The title compond is synthesized as described for 3-N-terf-butoxycarbonyl-aminobenzyi-4- nitrophenyl-carbonate (Example 1 b)), starting from 2-(4-methyl-5-thiazolyl)-ethanol (Aldrich, Buchs, Switzerland). Rf= 0.72 (chloroform:methanol:water:acetic acid = 850:130:15:5, v/v/v/v). canιple_9 2-(3-Hydroxyphenyl)ethyloxycarbonyl-Tyr(Pθ3H2)-πe-Asn-Gln-NH2 (SEQ ID NO: 9) In the final reaction step, the Λ/-terminal group is coupled as 2-(3-tert-butoxycarbonyl-oxy- phenyl)-ethyl-4-nitrophenyl-dicarbonate. Title compound: Mass spectral analysis (negative- ion mode): 778.4 (calc. 778.7, C33H45N7O13P1), tR= 6.44 min (HPLC System A). The starting material is prepared as follows: a) 2-(3-tert-Butoxycarbonyloxyphenyl)-ethanol A suspension of 2-(3-hydroxyphenyl)ethanol (3.7 g, 29.8 mmol; Fluka, Buchs, Switzerland)) and potassium carbonate (6 g, 43.4 mmol) in dichloromethane (6 ml) is cooled in an ice¬ water; di-tert-butyl-dicarbonate (6.54 g, 30 mmol) and 18-crown-6 (Aldrich, Buchs, Switzerland) are added and the mixture is allowed to warm up to room temperature under vigorous stirring. Stirring is continued overnight. The solution is extracted with brine, dried over Na2SO4 and dried in vacuo. The crude compound is subjected to flash chromato¬ graphy on silica gel using dichloromethane/methanol (95:5, v/v) as eluent. Rf= 0.66 (chloroform:methanol:water:acetic acid = 850:130:15:5, v/v/v/v). b) 2-(3-tert-butoxycarbonyl-oxyphenyl)ethyl-4-nitrophenyl-carbonate The title compound is synthesized in analogy to the method described for 3-N-tert-butoxy- carbonyl-aminobenzyl-4-nitrophenyl-carbonate (Example 1 b)), starting from 2-(3-tert- butoxycarbonyloxy-phenyl)ethanol: R = 0,81 (chloroform:methanol = 95:5, v/v). Example 10: 3-Hydroxybenzyloxycarbonyl-Tyr(PO3 H2H le-Asn-Gln-N H2 (SEQ ID NO: 10) The Λ/-terminai group is coupled as 3-(tert-butoxycarbonyl-oxy)-benzyl-4-nitrophenyi- dicarbonate. Title compound: Mass spectral analysis (negative-ion mode): 764.8 (calc. 764.7, C32H43N 7 Oι 3 P-|), t R = 6.57 min (HPLC System A). The starting material is prepared as follows: a) 3-0-ter,-Butoxycarbonyl-oxybenzyl-4-nitrophenyl-carboπate 3-O-te/t-butoxycarbonyl-oxybenzyl-4-nitrophenyl-carbonate is synthesized as described for 3-N-fert-butoxycarbonyl-aminobenzyl-4-nitrophenyl-carbonate (Example 1 b), starting from 3-hydroxybenzyl alcohol (Fluka, Buchs, Switzerland). Rf= 0.81 (chloroform:methanol:wa- ter:acetic acid = 850:130:15:5, v/v/v/v). Example 1 1 : 3-Aminobenzyloxycarbonyl-Tyr(Pθ3H2)-AcβC-βAla-NH2 (TFA salt) (SEQ ID NO: 11) Titie compound: Mass spectral analysis (negative-ion mode): 604.1 (calc. 604.6, C27H35N5O9P1), tR= 5.43 min (HPLC System A). Example 12: 3-Aminobenzyloxycarbonyl-Tyr(PO3H2)-Ac6C-Gly-NH2 (TFA salt) (SEQ ID NO: 12) Title compound: Mass spectral analysis (negative-ion mode): 590.5 (calc. 590.6, C26 H 33 N 5°9 P 1). *R= 5.93 min (HPLC System A). ajτιr j le_13: Benzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 13) Titie compound: Mass spectral analysis (negative-ion mode): 748.6 (calc. 748.7, c 32H43N7θ 1 Pι), t R = 7.37 min (HPLC System A). Example 14: 3,5-Diaminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 14) The N-terminal group is coupled as 3,5-di-tert-butoxycarbonyl-diaminobenzyl-4-nitrophenyl- dicarbonate. Title compound: Mass spectral analysis (negative-ion mode): 778.8 (calc. 778.7, C32H45Ν9O12P-1), t R = 4.69 min (HPLC System A). The starting material is prepared as follows: a) 3,5-N,N-di-tert-Butoxycarbonyl-aminobenzyl-4-nitrophenyl-carbonate The title compound is synthesized as described for 3-N-tert-butoxycarbonyl-aminobenzyl-4- nitrophenyl-carbonate (Example 1 b)), starting from 3,5-diaminobenzyl alcohol (Aldrich, Buchs, Switzerland, 2 HCI form. Rf= 0.71 (chloroform:methanol:water:acetic acid = 850:130:15:5, v/v/v/v). Exanπβ!e_15: 3-(3-lndolyl)propionoyl-Tyr(Pθ3H2)-lle-Asn-Gln-NH2 (SEQ ID NO: 15) 3-(3-indole)-propionic acid (Aldrich, Buchs, Switzerland) is coupled with BOP/HOBt (1 :1 ; 10 equiv.) in the presence of diisopropylethylamine (25 equiv.) in Λ/-methylpyrrolidin-2-one, yielding the title compound: Mass spectral analysis (negative-ion mode): 786.6 (calc. 785.8, C 35 H 46 N 8°11 P 1). R= 7.11 min (HPLC System A). Example 16: 3-.N-Acetylamino)phenoxvacetyl-Tyr(PO3H2.-He-Asn-Gln-NH2 (SEQ ID NO 16) 3-(N-Acetylamino)-phenoxy-acetic acid (2 equiv.) is coupled with BOP/HOBt (1 :1 ; 2 equiv.) in the presence of diisopropylethylamine (4 equiv.) in Nmethylpyrrolidin-2-one, yielding the title compound: Mass spectral analysis (negative-ion mode): 805.7 (calc. 805.8, C3 4 H 46 N8θι 3 Pι), tR= 6.02 min (HPLC System A). The starting material is prepared as follows: a) 3-(N-Acetylamino)phenoxy-acetic acid (= 3- (N-acetamido) phenoxyacetic acid) NaOH (2.08 g; 52 mmol; Fluka, Buchs, Switzerland) and chloroacetic acid (2.46 g, 26 mmol) are added to a solution of m-(acetylamino)-phenol (4.0 g, 26 mmol; Fluka, Buchs, Switzerland) in water (10 ml). The solution is incubated under reflux conditions for 1.5 h, and a further quantity of NaOH (1.04 g ) and chloroacetic acid (1.23 g) is added. 2.5 h later, the solution is cooled to room temperature and acidified with a concentrated solution of HCI. The precipitate is filtered and crystallized from water, yielding the title compound: Rf= 0.38 (ethyl acetate: methanol = 4:1 (v/v) with 0.5 % acetic acid). Example 17: 4-(N-Acetylamino)phenoxyacetyl-Tyr(PO3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 17) The title compound is prepared using a procedure analogous to Example 16, starting from 4-(N-acetylamino)phenoxy-acetic acid: Mass spectral analysis (negative-ion mode): 805.7 (calc. 805.8, C34H46N8O13P1), -R= 5.73 min (HPLC System A). The starting material is obtained as follows: a) 4-(N-Acetylamino)phenoxy-acetic acid The title compound is prepared in analogy to the method described for N-(3-acetylamino)- phenoxy-acetic acid (Example 16 a)): R f = 0.42 (ethyl acetate: methanol = 4:1 (v/v), with 0.5 % acetic acid). Example 18: N-(2-Acetvlamino)phenoxvacetyl-Tyr(Pθ3H2)-lle-Asn-Gln-NH2 (SEQ ID NO: 18) The title compound is prepared using a procedure analogous to the method in Example 16, starting from 2-(N-acetylamino)phenoxy-acetic acid: Mass spectral analysis (negative-ion mode): 805.8 (calc. 805.8, C34H46N 8 Oι 3 Pι), t R = 6.92 min (HPLC System A). The starting material is obtained as follows: a) 2-(N-Acetylamino)phenoxy-acetic acid The title compound is synthesized in analogy to the method described for 3-(N- acetylamino)phenoxy-acetic aicd (Example 16 a)): R f = 0.47 (ethyl acetate:methanol = 3:2 (v/v) with 0.5 % acetic acid). ExanτBle_19 4-Aminophenoxyacetyl-Tyr(Pθ3H2)-lle-Asn-Gln-NH2 (SEQ ID NO: 19) 4-(N-tert-butoxycarbonyl-amino)-phenoxyacetic acid (3 equiv.) is coupled with BOP/HOBt (1 :1 ; 3 equiv.) in the presence of diisopropylethylamine (7 equiv.) in Λ/-methylpyrrolidin-2- one (double coupling). Title compound: Mass spectral analysis (negative-ion mode): 763.5 (calc. 763.7, C32H44N80-I2P1), t R = 5.15 min (HPLC System A). The starting material is obtained as follows: a) 4-(N-tert-Butoxycarbonylamino)phenoxy-acetic acid A solution of 4-(N-acetylamino)phenoxy-acetic acid (Example 17 a)) (1.99 g, 8.77 mmol) in water (8 ml) and concentrated HCI (37 %, 8 ml) is refluxed for 2.5 h. The solution is cooled in an ice bath, and the precipitate is filtered. Incorporation of of the Boc group at the free amino group is carried out as described for 3-(N-tert-butoxycarbonyl)aminobenzyl alcohol (Example 1 a)), yielding the title compound: R f = 0.58 (ethyl acetate:methanol = 3:1 (v/v) with 0.5 % acetic acid). Example 20: 3-Aminophenoxyacetvl-Tvr(Pθ3H2--He-Asn-Gln-NH2 (TFA salt) The title compound is prepared using a procedure analogous to Example 19, starting from 3-(N-tert-butoxycarbonylamino)phenoxy-acetic acid. Mass spectral analysis (negative-ion mode): 764.0 (calc. 763.7, C32H44N8O12P1), -R= 4.92 min (HPLC System A). The starting material is obtained as follows: a) 3-(N-tert-Butoxycarbonylamino)phenoxy-acetic acid The title compound is synthesized as described for 4-(N-tert-butoxycarbonylamino)phenoxy- acetic acid (Example 19 a)), starting from 3-(N-Acetylamino)phenoxy-acetic acid (Example 16 a)): R f = 0.66 (ethyl acetate:methanol = 3:1 (v/v) with 0.5 % acetic acid). ajτmJe_ 1ι 4-(3-lndolyl)butyrolyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 21) The title compound is prepared using a protocol analogous to Example 16 with 4-(3- indolyl)butyric acid (Aldrich, Buchs, Switzerland). Mass spectral analysis (negative-ion mode): 799.4 (calc. 799.8, C 36 H4 8 N 8 0-| i Pι), t R = 7.49 min (HPLC System A). Example 22: S-lndolvl-acetvl-TvrfPOgHo He-Asn-Gln-NHo (SEQ ID NO: 22) The title compound is prepared using a protocol analogous to Example 16 with 3-indolyl- acetic acid (Aldrich, Buchs, Switzerland). Mass spectral analysis (negative-ion mode): 773.0 (calc. 771.8, C34H44N8O11 P-| ), t R = 6.73 min (HPLC System A). Example 23: Benzovl-TvrfPOgHo He-Asn-Gln-NHo (SEQ ID NO: 23) The title compound is prepared using a protocol analogous to Example 16. Mass spectral analysis (negative-ion mode): 718.4 (calc. 718.7, C31 H41 N7O11 P-1), t = 6.25 min (HPLC System A). Example 24: 4-Aminobenzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 24) (4-tert-Butoxycarbonyl-amino)-benzoic acid (2 equiv.) is coupled with BOP/HOBt ( 1 :1 ; 2 equiv.) in the presence of diisopropylethylamine (4 equiv.) in Λ/-methylpyrrolidin-2-one. Title compound: Mass spectral analysis (negative-ion mode): 733.5 (calc. 733.7, C31 H 42 N 8 0ι 1 Pi), tR= 4.57 min (HPLC System A). The starting material is obtained as follows: a) (4-tert-Butoxycarbonyl-amino)-benzoic acid The title compound is synthesized in analogy to the method described for 3-N-tert-butoxy- carbonylamino-benzyl alcohol (Example 1 a) ), starting from 4-amino benzoic acid (Aldrich, Buchs, Switzerland): R f = 0.37 (chloroform:methanol:water:acetic acid = 850:130:15:5, v/v/v/v). Example 25: Benzimidazol-5-ylcarbony!-Tyr(Pθ3 H2H le-Asn-Gln-N H2 (SEQ ID NO: 25) 5-Benzimidazole-carboxylic acid (Aldrich, Buchs, Switzerland) is coupled with BOP/HOBt (1 :1 ; 3 equiv.; first coupling) in the presence of diisopropylethylamine (7 equiv.) and with O- (7-azabenzotriazol-1-yl)-1 ,1 ,3,3-bis(tetramethyiene)uronium hexafluorophosphate (3 equiv.; second coupling) in the presence of diisopropylethylamine (7 equiv.). Title compound: Mass spectral analysis (negative-ion mode): 758.4 (calc. 758.7, C32H41 N9O11 P1), t = 4.91 min (HPLC System A). Example 26: 2-Amino-thiazol-4-yl-acetyl-Tyr(Pθ3H )-lle-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 26) The compound is prepared using a protocol analogous to Example 16, using 2-amino- thiazol-4-yl-acetic acid (Aldrich, Buchs, Siwtzerland). Title compound: Mass spectral analysis (negative-ion mode): 754.7 (calc. 754.8, C29H41 N9O11 P1 S1 ), .R= 4.51 min (HPLC System A). Bcajτιpje_27l 4-Cyanobenzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 27) The compound is prepared using a protocol analogous to Example 25, using 4-cyano- benzoic acid (Fluka, Buchs, Switzerland). Title compound: Mass spectral analysis (negative- ion mode): 743.9 (calc. 743.7, C32H 40 N 8 Oι 1 P-|), t R = 6.44 min (HPLC System A). Examr j le_28ι_2,3-Dihydrobenzofuran-5-carbonyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 28) The compound is prepared using a protocol analogous to Example 25, using 2,3- dihydobenzofuran-5-carboxylic acid (Maybridge, Cornwall, USA). Title compound: Mass spectral analysis (negative-ion mode): 760.6 (calc. 760.7, C33H43N7O12P1). tR= 6.36 min (HPLC System A). Example 29: 4-Hvdroxybenzovl-Tvr(Pθ3HoHle-Asn-Gln-NH2 (SEQ ID NO: 29) The compound is prepared using a protocol analogous to Example 25, using 4-hydroxy benzoic acid (Fluka, Buchs, Switzerland). Title compound: Mass spectral analysis (negative- ion mode): 734.6 (calc. 734.7, C3i H4i N 7 0ι 2 Pι), tR= 5.49 min (HPLC System A). cajϊiBle_3P 4-Methoxybenzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 30) The compound is prepared using a protocol analogous to Example 25, using 4-methoxy- benzoic acid (Fluka, Buchs, Switzerland). Title compound: Mass spectral analysis (negative- ion mode): 748.9 (calc. 748.7, C32H43N7O12P1), -R= 6.65 min (HPLC System A). Example 31 : 4-Methvlthiobenzovl-Tvr(Pθ3H )-lle-Asn-Gln-NH2 (SEQ ID NO: 31) The compound is prepared using a protocol analogous to Example 25, using 4-methylthio- benzoic acid (Fluka, Buchs, Switzerland). Title compound: Mass spectral analysis (negative- ion mode): 764.6 (calc. 764.8, C32H43 7O1 ■ ) P-| S-|), t R = 7.21 min (HPLC System A). B<aιnpje_32: 4-Methylsulfinyl-benzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 32) The compound is obtained by oxidation of the title compound of Example 31 with 5 % hydrogen peroxide at room temperature; the course of the reaction is monitored by HPLC (System A). After 45 min, the starting material has been converted to the sulfoxide deri¬ vative. The solution is then concentrated to dryness and lyophilized from 80 % acetic acid. Title compound: Mass spectral analysis (negative-ion mode): 780.5 (calc. 780.8, C32H43N7O12P1 S1), tR= 7.09 min (HPLC System A). Example 33: trans-(4-lmidazolyl-acryloyl)-Tyr(P0 3 H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 33) The compound is prepared using a protocol analogous to Example 25, using trans-4-imida- zoleacrylic acid (Aldrich, Buchs, Switzerland)). Title compound: Mass spectral analysis (ne¬ gative-ion mode): 735.1 (calc. 734.7, C30H41 N9O11 P-1), tR= 4.41 min (HPLC System A). Example 34: 4-(N-Methylamino)benzovl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 34) The compound is prepared using a protocol analogous to Example 25, using 4-(N-methyl- amino)benzoic acid (Fluka, Buchs, Switzerland). Title compound: Mass spectral analysis (negative-ion mode): 748.4 (calc. 747.7, C32H44N8O11 P-|), t = 4.97 min (HPLC System A). BcaιnpJe_35ι 4-(N,N-Dimethylamino)benzoyl-Tyr(Pθ3H2)-lle-Asn-Gln-NH2 (SEQ ID NO: 35) The compound is prepared using a protocol analogous to Example 25, using 4-(N,N-di- methylamino)benzoic acid (Fluka, Buchs, Switzerland). Title compound: Mass spectral analysis (negative-ion mode): 761.7 (calc. 761.8, C33H46N8O11 P1), .R= 5.41 min (HPLC System A). Exarnr j le_36: Pyridin-4-carbonyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 36) The compound is prepared using a protocol analogous to Example 25, using pyridin-4- carbonic acid (Fluka, Buchs, Switzerland). Title compound: Mass spectral analysis (nega¬ tive-ion mode): 719.9 (calc. 719.7, C3oH 4 oN 8 0- | 1 P- j ), .R= 4.21 min (HPLC System A). Example 37: 4-Aminomethylbenzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 37) The compound is prepared using a protocol analogous to Example 25, using 4-aminome- thyl-benzoic acid (Fluka, Buchs, Switzerland). Title compound: Mass spectral analysis (ne¬ gative-ion mode): 747.9 (calc. 747.7, C32H44N8O11 P-|), tR= 4.39 min (HPLC System A). Example 38: 4-Amino-3-methoxybenzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 38) The compound is prepared using a protocol analogous to Example 25, using 4-amino-3- methoxybenzoic acid (Aldrich, Buchs, Switzerland). Title compound: Mass spectral analysis (negative-ion mode): 764.4 (calc.763.7, C32H44N8O12P1). *R= 4.59 min (HPLC System A). Example 39: 4-Aminophenylacetyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 39) The compound is prepared using a protocol analogous to Example 25, using 4-aminophenyl acetic acid (Aldrich, Buchs, Switzerland). Title compound: Mass spectral analysis (negative- ion mode): 748.4 (calc. 747.7, C32H44N8O1 - j P-|), t R = 4.89 min (HPLC System A). Example 40: 3-Aminobenzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 40) 3-(tert-Butoxycarbonyl-amino)benzoic acid (3 equiv.) is coupled with BOP/HOBt (1 :1 ; 3 equiv.) in the presence of diisopropylethylamine (7 equiv.) in Λ/-methylpyrrolidin-2-one. Title compound: Mass spectral analysis (negative-ion mode): 733.3 (calc. 733.7, C31 H 42 N 8 0ι 1 Pi), t R = 4.42 min (HPLC System A). The starting material is prepared as follows: a) 3-(tert-Butoxycarbonyl-amino)benzoic acid The title compound is synthesized in analogy to the method described for 3-N-tert-butoxy- carbonyl-aminobenzyl alcohol (Example 1 a)), starting from 3-aminobenzoic acid (Fluka, Buchs, Switzerland): R f = 0.48 (chloroform:metanol:water:acetic acid = 850:130:15:5 (v/v/v/v)). Example 41 : Quinoline-6-vlcarbonvl-Tvr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 41) The compound is prepared using a protocol analogous to Example 25, using quinoline-6- carboxylic acid (Fisher Scientific, Pittsburg, USA). Title compound: Mass spectral analysis (negative-ion mode): 769.8 (calc. 769.7, 034^2^01 -1 P- j ), tR= 4.88 min (HPLC System A). & aiχτple_42 4-Methoxycarbonylbenzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 42) The compound is prepared using a protocol analogous to Example 25, using 4-methoxy- carbonylbenzoic acid (= monomethyl terephthalate, Fluka, Buchs, Switzerland). Title compound: Mass spectral analysis (negative-ion mode): 776.9 (calc. 776.7, C33H43N7O-13P1), tR= 6.78 min (HPLC System A). Example 43: 4-Carboxybenzoyl-Tyr ( Pθ3H )-lle-Asn-Gln-NH2 (SEQ ID NO: 43) The compound is obtained by saponification of the title compound of Example 42 with sodium hydroxide as follows: 4-Methoxycarbonylbenzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 42) (27 mg, 35 μmol) is dissolved in 2.7 ml of water and 34.7 μl of a 1 N solu¬ tion of NaOH is added. The course of the reaction is followed by anayltical HPLC. After 2 h, a further 312 μl of 1 N NaOH are added. After disappearance of the starting material (15 min), the solution is neutralized with 2N HCI (174 μl) and injected directly into the Medium Pressure Liquid Chromatography system described in Example 1 for purification. Title compound: Mass spectral analysis (negative-ion mode): 762.7 (calc. 762.7, c 32H4i N 7 0ι 3 P-|), t R = 6.81 min (HPLC System A). Example 44: 4-Amino-2-chlorobenzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 44) The compound is prepared using a protocol analogous to Example 16, using 4-amino-2- chlorobenzoic acid (Aldrich, Buchs, Switzerland). Title compound: Mass spectral analysis (negative-ion mode): 768.1 (calc. 768.2, C3 1 H 4 - ( N8θ 1 -| P-( Clι ), tR= 4.59 min (HPLC System A). Example 45: 6-Amino-nicotinoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 45) The compound is prepared using a protocol analogous to Example 16, using 6-amino-nicoti- nic acid (Fluka, Buchs, Switzerland). Title compound: Mass spectral analysis (negative-ion mode): 734.7 (calc. 734.7, C30H41 NgO- j 1 P- | ). Purity control is made with reversed-phase analytical HPLC on a Nucleosil C 18 -column (Macherey & Nagel, Dϋren, FRG; 250 x 4 mm, 5 μm, 100 A); linear gradient over 10 min of MeCN/0.09% TFA and H 2 O/0.1% TFA from 5:95 to 13:7, flow rate 1.5 ml/min, detection at 215 nm (HPLC System B): tR= 4.77 min. Example 46: 4-Amino-3-hydroxybenzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 46) The compound is prepared using a protocol analogous to Example 16, using 4-amino-3- hydroxybenzoic acid (Fluka, Buchs, Switzerland). Title compound: Mass spectral analysis (negative-ion mode): 749.5 (calc.749.7, C31 H42N8O12P1). R= 5.51 min (HPLC System B). Example 47: 3-(3-Aminophenyl)propionoyl-Tyr(Pθ3H2)-He-Asn-Gin-NH2 (TFA salt) (SEQ ID NO: 47) 3-(3-Aminophenyl)propionic acid (3 equiv.; Trans World Chemicals, Rockville, USA) is coupled with BOP/HOBt (1 :1 ; 3 equiv.) in the presence of diisopropylethylamine (7 equiv.) in /V-methylpyrroiidin-2-one. Title compound: Mass spectral analysis (negative-ion mode): 761.8 (calc. 761.8, C 33 H 46 N 8 0ι -| Pi). .R= 5.22 min (HPLC System B). Example 48: 4-Aminobenzoyl-Tyr(Pθ3H2)-He-NH2 (TFA salt) (SEQ ID NO: 48) 4-(tert-butoxycarbonyl-amino)benzoic acid (2 equiv.) is coupled with BOP/HOBt (1 :1 ; 2 equiv.) in the presence of diisopropylethylamine (4 equiv.) in Λ/-methylpyrrolidin-2-one. Title compound: Mass spectral analysis (negative-ion mode): 491.3 (calc. 491.5, C22 H 28 N 4°7 P 1). *R= 4.84 min (HPLC System A). The starting material is prepared as follows: a) 4-(tert-Butoxycarbonylamino)benzoic acid The title compound is prepared using a protocol analogous to that for synthesis of 3-N-tert- butoxycarbonyl-aminobenzyl alcohol (Example 1 a)), starting with 4-amino-benzoic acid (Fluka, Buchs, Switzerland): R f = 0.38 (chloroform:methanol:water:acetic acid = 850:130:15:5, v/v/v/v)). Example 49: trans-(3-lndolvl-acrvlovn-Tvr(PO3H2l-lle-Asn-Gln-NH (SEQ ID NO: 49) trans-3-lndolyl-acrylic acid (Fluka, Buchs, Switzerland) is coupled with BOP/HOBt (1 :1 , 3 equiv.; first coupling) and N-[(dimethylamino)-1H-1 ,2,3-triazolo[4,5-b]pyridin-1-ylmethylene]- N-methylmethanaminium hexafluorophosphate N-oxide (3 equiv.; second coupling) in the presence of diisopropylethylamine (6 equiv.).. Title compound: Mass spectral analysis (negative-ion mode): 783.6 (calc. 783.8, C35H44N8O11 P- | ), tR= 4.32 min (HPLC System A). Example 50: 4-Aminobenzoyl-Tyr(Pθ3H2)-He-Asn-NH2 (TFA salt) (SEQ ID NO: 50) (4-te ?-Butoxycarbonyl-amino)benzoic acid (Example 48 a)) is coupled with BOP/HOBt (1 :1 , 3 equiv., double coupling) in the presence of diisopropyl ethylamine (6.0 equiv.). Title compound: Mass spectral analysis (negative-ion mode): 605.3 (calc. 605.6, C 26 H 34 N 6°9 P 1). tR= 4 - 53 in (HPLC System A). Example 51 : 4-Aminobenzoyl-Tyr(Pθ3H2)-Asp-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 51) The compound is prepared using a protocol analogous to Example 50. Title compound: Mass spectral analysis (negative-ion mode): 735.9 (calc. 735.6, C29H36N8O13P1), tR= 5.15 min (HPLC System C = reversed-phase analytical HPLC on a Nudeosil Cι 8 column (250 x 4 mm, 5 μm, 100 A; Macherey & Nagel, Dϋren, FRG); linear gradient over 10 min of acetonitrile/0.09% TFA and H 2 O/0.1 % TFA from 0:1 to 23:77, flow rate 2.0 ml/min, detection at 215 nm). Example 52: 4-Aminobenzoyl-Tyr(P0 3 H 2 )-Gly-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 52) The compound is prepared using a protocol analogous to Example 50. Title compound: Mass spectral analysis (negative-ion mode): 678.0 (calc. 677.6, C27H34N8O11 P1), t R = 4.87 min (HPLC System C). Example 53: 4-Aminobenzoyl-Tyr(PO 3 H2)-lle-Asn-Gly-NH (TFA salt) (SEQ ID NO: 53) The compound is prepared using a protocol analogous to Example 50. Title compound: Mass spectral analysis (negative-ion mode): 662.7 (calc. 662.6, C28H37N7O10P1). t R = 4.46 min (HPLC System A). Example 54: 4-Aminobenzoyl-Tyr(Pθ3H2)-He-Asn-Val-NH2 (TFA salt) (SEQ ID NO: 54) The compound is prepared using a protocol analogous to Example 50. Title compound: Mass spectral analysis (negative-ion mode): 705.1 (calc. 704.7, C31 H43N7O10P1). tR= 5.76 min (HPLC System A). Example 55: 4-Aminobenzoyl-Tyr(Pθ3H2)-He-Asn-Asp-NH2 (TFA salt) (SEQ ID NO: 55) The compound is prepared using a protocol analogous to Example 50. Title compound: Mass spectral analysis (negative-ion mode): 721.3 (calc. 720.7, C30H39N7O12P1). t R = 4.61 min (HPLC System A). Example 56: 4-Aminobenzoyl-Tyr(Pθ3H2)-He-Asn-Ac5C-NH2 (TFA salt) (SEQ ID NO: 56) The compound is prepared using a protocol analogous to Example 50. Title compound: Mass spectral analysis (negative-ion mode): 717.4 (calc. 716.7, C32H43N7O10P1). tR= 5.38 min (HPLC System A). Example 57: 4-Aminobenzoyl-Tyr(Pθ3H2)-He-Asn-Asn-NH2 (TFA salt) (SEQ ID NO: 57) The compound is prepared using a protocol analogous to Example 50. Title compound: Mass spectral analysis (negative-ion mode): 720.0 (calc. 719.7, C30H40N8O11 P1), tR= 4.36 min (HPLC System A). Example 58: 4-Aminobenzoyl-Tyr(Pθ3H2)-He-Asn-βAla-NH2 (TFA salt) (SEQ ID NO: 58) The compound is prepared using a protocol analogous to Example 50. Title compound: Mass spectral analysis (negative-ion mode): 676.9 (calc. 676.7, C29H39N7O10P1). tR= 4.68 min (HPLC System A). Example 59: 4-Aminobenzoyl-Tyr(Pθ3H2)-lle-Gly-Gln-NH2 (TFA salt) (SEQ ID NO: 59) The compound is prepared using a protocol analogous to Example 50. Title compound: Mass spectral analysis (negative-ion mode): 676.4 (calc. 676.6, C29H39N7O10 1). tR= 4.81 min (HPLC System A). Example 60: 4-Aminobenzoyl-Tyr(P03H 2 )-lle-Gln-Gln-NH2 (TFA salt) (SEQ ID NO: 60) The compound is prepared using a protocol analogous to Example 50. Title compound: Mass spectral analysis (negative-ion mode): 747.9 (calc. 747.7 C32H44N8O11 P-\), t R = 4.45 min (HPLC System A). Example 61 : lndole-5-vlcarbonyl-Tyr(P03H ^-lle-Asn-Gln-NH2 (SEQ ID NO: 61) The peptide is synthesized manually on a 4-(2',4'-dimethoxyphenyl-aminomethyl)-phenoxy resin, employing a procedure analogous to Example 1. The N-terminal group is incorporated as N-terf-butoxycarbonyl-indole-5-ylcarboxylic acid (3 equiv.) using benzotriazole- 1yl-N-oxy- tris-(dimethylamino)-phosphonium hexafluorophosphate/N-hydroxybenzotriazole (1:1 ; 3 equiv.) in the presence of diisopropylethylamine (7 equiv.) in N-methylpyrrolidin-2-one. The complete peptide resin obtained after the final coupling is simultaneosly deprotected- cleaved by treatment with trifluoro-acetic acid/ethanedithiol/H2θ (76:20:4, v/v/v) for 3 h at room temperature. The filtrate from the cleavage reaction is precipitated in diisopropyl ether-petroleum ether (1 :1 , v/v, 0 °C), and the precipitate collected by filtration. Decarboxylation of the resulting N-carboxy of the N-terminal indole ring is carried out in 0.1 M acetic acid (1 h at room temperature; see White, P, in Smith, J.A., Rivier, J.E. (eds.): Peptides, Chemistry and Biology, ESCOM, Leiden 1992, pp 537-538). The crude peptide is purified by medium-pressure liquid chromatography as described in Example 1. The title compound is obtained: Mass spectral analysis (negative-ion mode): 757.3 (calc. 757.7, C 33 H 42 N 8°11 P 1)' *R= 6 - 50 min (HPLC System B). The starting material is prepared as follows: a) N-tert-Butoxycarbonyl-indole-5-ylcarboxylic acid The methyl ester of 5-indolecarboxylic acid is prepared as described in J. Org. Chem. 42, 1286 (1977), having an R = 0.66 (chloroform:methanol:water:acetic acid = 850:130:15:5, v/v/v/v). N-tert-butoxycarbonyl-indole-5-ylcarboxylic acid is prepared as decribed in J. Chem. Soc, Chem. Commun. 1984. 1699, the titie compound being characterized by an R f = 0.56 (chloroform:methanol:water:acetic acid = 850:130:15:5, v/v/v/v). B a τiB]ej62: lndole-5-yicarbonyl-Tyr(Pθ3H2)-lle-Asn-NH2 (SEQ ID NO: 62) The compound is prepared using a procedure analogous to Example 61. Title compound: Mass spectral analysis (negative-ion mode): 629.5 (calc. 629.6, C28H34N6O9P1). t R = 6.86 min (HPLC System B). Example 63: lndole-5-ylcarbonvl-Tvr(PQ3H2)-Acfic-Asn-Gln-NH2 (SEQ ID NO: 63) The compound is prepared using a procedure analogous to Example 61. Title compound: Mass spectral analysis (negative-ion mode): 769.7 (calc. 769.7, C34H42N8O11 P1). t R = 6.53 min (HPLC System B). Example 64: 3-Aminobenzyloxycarbonyl- -F2Pmp-lle-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 64) The peptide is synthesized manually on a 4-(2',4'-dimethoxyphenyl-aminomethyl)-phenoxy resin, employing a procedure analogous to Example 1. Incorporation of N α -Fmoc-[4-(0- diethyl)-phosphono(difluoromethyl)]-L-phenylalanine (for synthesis see Tetrahedron Lett. 34(22), 3543 (1993)) to the protected peptide resin is carried out with benzotriazole-1yl-N- oxytris-(dimethylamino)-phosphonium hexafluorophosphate/N-hydroxybenzotriazole (1 :1 ; 3 equiv.) in the presence of diisopropylethylamine (7 equiv.), 3 h reaction time. After removal of the N-terminal Fmoc group, the peptide resin is treated with 1 M trimethylsilyltrifluoro- methane sulfonate-2 M dimethylsulfide-trifluoroacetic acid (500 ml to 0.005 mmol of NH2)- ethanedithiol (100 ml)-m-cresol (25 ml) 30 min at 4 °C and 3.5 h at room temperature (see Tetrahedron Lett. 34(44), 7093 (1993). The filtrate from the cleavage reaction is precipitated in diisopropyl ether-petroleum ether (1:1 , v/v, 0 °C), and the precipitate collected by filtration. The crude peptide is purified by medium-pressure liquid chromatography as described in Example 1. The crude title compound in Boc-protected form is obtained by reaction of H- .-F2Pmp-lle-Asn-Gln-NH2 (1 equiv.) with 3-tert-butoxycarbonyl-aminobenzyl- 4-nitrophenyl-carbonate (see Example 1 b)) (3 equiv.) in the presence of diisopropylethylamine (3 equiv.). The crude product is purified by medium-pressure liquid chromatography as described in Example 1. The tert-butoxycarbonyl group of the N- terminal moiety is removed with trifluoroacetic acid/water (95:5, v/v), and the title compound is obtained: Mass spectral analysis (negative-ion mode): 797.6 (calc 797.7, c 33 H 44 8O-| -j P-j F 2 ), t R = 5.43 min (HPLC System A). Examle 65: 4-Aminobenzoyl- -F2Pmp-lle-Asn-Gln-NH2 (TFA salt) (SEQ ID NO: 65) The peptide is synthesized manually on a 4-(2',4'-dimethoxyphenyl-aminomethyl)-phenoxy resin, employing a procedure analogous to Example 1. Incorporation of N α -Fmoc-[4-(O-di- ethyl)-phosphono(difluoromethyl)]-L-phenylalanine (reference: see Example 64) to the pro¬ tected peptide resin is carried out as in Example 64. (4-tert-butoxycarbonyl-amino)-benzoic acid (Example 48 a)) (3 equiv.) is coupled with BOP/HOBt (1 :1 ; 3 equiv.) in the presence of diisopropylethylamine (7 equiv.) in Λ/-methylpyrrolidin-2-one. After completion of the syn¬ thesis, the peptide resin is treated with 1 M trimethylsilyltrifiuoro-methane sulfonate-2 M dimethylsulfide-trifluoroacetic acid (500 ml to 0.005 mmol of NH2)-ethanedithiol (100 m\)-m- cresol (25 ml) 30 min at 4 °C and 3.5 h at room temperature. The filtrate from the cleavage reaction is precipitated in diisopropyl ether-petroleum ether (1 :1 , v/v, 0 °C), and the preci¬ pitate collected by filtration. The crude peptide is purified by medium-pressure liquid chro¬ matography as described in Example 1. Title compound: Mass spectral analysis (negative- ion mode): 768.1 (calc. 767.7, C32H42N 8 Oι 0 Pι F2), .R= 4.86 min (HPLC System A). Example 66: 4-Aminobenzoyl- Tyr(P0 3 H 2 )-Phe-Asn-Gln-NH2 (TFA Salt) (SEQ ID NO: 66) The title compound is prepared analogously to Example 50: Mass spectral analysis (negative ion mode): 767.9 (calc. 767.7, C 34 H 0 N 8 OnPι); t R = 5.0 min (HPLC System A). Example 67: Trans-3.4-dihydroxv-cinnamovl-Tvr(Pθ3H,>)-He-Asn-Gln-NH2 (SEQ ID NO: 67) The peptide is synthesized manually on a 4-(2',4'-dimethoxyphenyl-aminomethyl)-phenoxy- resin (Novabiochem, Laufelfingen, Switzerland), employing the fluorenylmethoxycarbonyl strategy. Fmoc-removal is with piperidine/dimethylacetamide (1 :4, v/v; 6 x 2 min), followed by washing with methanol (3 x 1 min), Λ/-methylpyrrolidin-2-one (2 x 1 min), methanol (3 x 1 min), and Λ/-methylpyrrolidin-2-one (3 x 2 min). Coupling is achieved by first dissolving the Fmoc-amino acid (2 equiv.), diisopropylethylamine (2.2 equiv.), and the 2-(2-pyridon-1-yl)- 1 ,1 ,3,3-tetramethyluronium tetrafluoroborate reagent (2 equiv.) in Λ/-methylpyrrolidin-2-one, then waiting 3 min for preactivation, adding the mixture to the resin, and finally shaking for at least 45 min. Asparagine and glutamine side chains are protected with the trityl group. The incorporation of N α -Fmoc-Tyr(P0 3 H2)-OH (3 equiv.) is accomplished with benzo- tri izole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxybenzo- triazole (1 :1 ; 3 equiv.; first coupling) and N-[(dimethylamino)-1 H-1 ,2,3-triazolo[4,5-b]pyridin- 1-ylmethylene]-N-methylmethanaminium hexafluorophosphate N-oxide (3 equiv.; second coupling) in the presence of diisopropylethylamine (7 equiv.). trans-3,4-Dihydroxy-cinnamic acid (2 equiv.; Fluka, Buchs, Switzerland) is incorporated (double coupling) with benzotri- azole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxybenzo- triazole (1 :1 ; 3 equiv.) in the presence of diisopropylethylamine (4 equiv.). The complete peptide resin obtained after the last coupling step is simultaneosly deprotected and cleaved by treatment with trifluoroacetic acid/H 2 0 (95:5, v/v) for 3 h at room temperature. The filtrate from the cleavage reaction is precipitated in diisopropyl ether/petroleum ether (1 :1 , v/v, 0 °C), and the precipitate collected by filtration. The crude peptide is purified by medium-pres¬ sure liquid chromatography using a Cι 8 -column (Merck LICHROPREP RP-18, 15-25 μm bead diameter, reversed phase material based on Cis'derivatized silicagel, Merck, Darm¬ stadt, FRG; column length 46 cm, diameter 3.6 cm; flow rate 53.3 ml/min; detection at 215 nm) eluted with an acetonitrile-water gradient containing 0.1 % of TFA. The title com¬ pound is obtained: Mass-spectral analysis (matrix-assisted laser-desorption ionization time- of-flight mass spectrometry, MALDI-TOF) reveals a molecular mass within 0.1 % of the expected value (negative-ion mode): 776.6 (calc. 776.7, C33H43N7O13P1). The purity of the peptide is verified by reversed-phase analytical HPLC on a Nudeosil Cι 8 -column (250 x 4 mm, 5 μm, 100 A): linear gradient over 10 min of MeCN/0.09% TFA and H 2 O/0.1% TFA from 1 :49 to 3:2; flow rate 2.0 mLJmin, detection at 215 nm (HPLC system A), single peak at tR= 5.29 min. In analogy to example 67, the following examples 68 to 122 are obtained, if not described otherwise: Example 68: trans-3-Hydroxv-cinnamoyl-Tvr(PO.'-;H?)-He-Asn-Gln-NH9 (SEQ ID NO: 68) trans-3-Hydroxy-cinnamic acid is from Fluka (Buchs, Switzerland) and is used without side- chain protection. Title compound: Mass-spectral analysis (negative-ion mode): 760.8 (calc. 760.7, C33H43N7O12P1). tR= 6.04 (HPLC system A). Example 69: trans-3-Hydroxy-4-methoxv-cinnamoyl-Tvr(P03Hp)-lle-Asn-Gln-NHp (SEQ ID NO: 69) trans-3-Hydroxy-4-methoxy-cinnamic acid is from Janssen (Olen, Belgium) and is used without side-chain protection. Title compound: Mass-spectral analysis (negative-ion mode): 790.1 (calc. 790.7, C34H45N7O13P1). tR= 5.77 (HPLC system A). Example 70: trans-3.4-Dihvdroxy-cinnamovl-Tvr(POqHp)-lle-NHp (SEQ ID NO: 70) trans-3,4-Dihydroxy-cinnamic acid (3 equiv.) is incorporated with benzotriazole-1-yl-oxy-tris- dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxybenzotriazole (1:1 ; 3 equiv.; first coupling) and N-[(dimethylamino)-1 H-1 ,2,3-triazolo[4,5-b]pyridin-1-ylmethylene]-N- methylmethanaminium hexafluorophosphate N-oxide (3 equiv.; second coupling) in the presence of diisopropylethylamine (7 equiv.). Title compound: Mass-spectral analysis (negative-ion mode): 534.4 (calc. 534.5, C24H29N3O9P1). tR= 6.45 (HPLC system A). Example 71 : trans-3.4-Dihvdroxv-cinnamoyl-Tvr(Pθ3H.>)-AcfiC-NH;> (SEQ ID NO: 71) trans-3,4-Dihydroxy-cinnamic acid (3 equiv.) is incorporated with benzotriazole-1 -yl-oxy-tris- dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxybenzotriazole (1 :1 ; 3 equiv.; first coupling) and N-[(dimethylamino)-1 H-1 ,2,3-triazolo[4,5-b]pyridin-1-ylmethylene]-N- methylmethanaminium hexafluorophosphate N-oxide (3 equiv.; second coupling) in the presence of diisopropylethylamine (7 equiv.). Titie compound: Mass-spectral analysis (negative-ion mode): 546.8 (calc. 546.5, C25H29N3O9P1). tR= 6.18 (HPLC system A). The starting material is prepared as follows: a) Fmoc-1 -amino-cvclohexanecarboxylic acid The title compound is synthesized starting from 1 -amino-cyclohexanecarboxylic acid (Janssen, Olen, Belgium) according to a procedure known in the art (see E. Atherton and R.C. Sheppard, in Solid-Phase Peptide Synthesis- A Practical Approach, eds.: D. Rickwood and B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989): R f = 0.84 (chloroform:methanol:water:acetic acid, 750:270:50:5, v/v/v/v). Example 72: trans-3.4-Dihydroxv-cinnamoyl-Tyr(POr.H9)-AcRC-Asn-NH9 (SEQ ID NO: 72) Mass-spectral analysis (negative-ion mode): 660.4 (calc. 660.6, C29H35N5O11 P1). tR= 5.86 (HPLC system A). The starting material is prepared as follows: a) Fmoc-1 -amino-cvclohexanecarboxylic acid The title compound is synthesized starting from 1 -amino-cyclohexanecarboxylic acid (Janssen, Olen, Belgium) according to a procedure known in the art (E. Atherton and R.C. Sheppard, in Solid-Phase Peptide Synthesis- A Practical Approach, eds.: D. Rickwood and B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989): R f = 0.84 (chloroform:methanol:water:acetic acid, 750:270:50:5, v/v/v/v). Example 73: 7.8-Dihvdroxy-2-oxo-2H-(benzopvran)-3-carboxvl-Tvr(Pθ3Hg)-lle-Asn-NH2 (SEQ ID NO: 7) Mass-spectral analysis (negative-ion mode): 689.7 (calc. 690.6, C29H33N5O13P1). Linear gradient over 10 min of MeCN/0.09% TFA and H 2 O/0.1 % TFA from 1 :19 to 13:7; flow rate 2.0 mLJmin, detection at 215 nm (HPLC system B), single peak at tR= 6.41. The starting material 7,8-dihydroxy-2-oxo-2H-(benzopyran)-3-carboxylic acid (3,4-dioxycu- marin carboxylic acid) is synthesized as described in the literature (see F. Vorsatz, J. Prakt. Chem., 145, 265-269 (1936)). Example 74: trans-3.4-Dihvdroxy-cinnamovl-Tvr(P03H9)-Met-Asn-NHg (SEQ ID NO: 74) trans-3,4-Dihydroxy-cinnamic acid (3 equiv.) is incorporated with benzotriazole-1-yl-oxy-tris- dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxybenzotriazole (1 :1 ; 3 equiv.; first coupling) and N-[(dimethylamino)-1 H-1 ,2,3-triazolo[4,5-b]pyridin-1-ylmethylene]-N- methylmethanaminium hexafluorophosphate N-oxide (3 equiv.; second coupling) in the presence of diisopropylethylamine (7 equiv.). The manual synthesis results in the title compound: Mass-spectral analysis (negative-ion mode): 666.6 (calc. 666.6, C-27H33N5O11P1S1). t R = 5.64 (HPLC system B). Example 75: trans-3,4-Dihydroxy-cinnamoyl-Tyr(Pθ3H2)-Pro-Asn-NH2 (SEQ ID NO: 75) The manual synthesis results in the title compound: Mass-spectral analysis (negative-ion mode): 632.4 (calc. 632.6, C27H31 N5O11 P1). tR= 4.83 (HPLC system A). Example 76: 3-(3,4-Dihvdroxvphenvl)-propionvl-Tvr(PQ.-:Hp)-lle-Asn-NHp (SEQ ID NO: 76) 3-(3,4-Dihydroxyphenyl)-propionic acid is from Fluka (Buchs, Switzerland) and is incorpora¬ ted with benzotriazole- 1 -yi-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hy- droxybenzotriazole (1 :1 ; 3 equiv.; first coupling) and N-[(dimethylamino)-1 H-1 ,2,3- triazolo[4,5-b]pyridin-1 -ylmethylene]-N-methylmethanaminium hexafluorophosphate N-oxide (3 equiv.; second coupling) in the presence of diisopropylethylamine (7 equiv.). The manual synthesis results in the title compound: Mass-spectral analysis (negative-ion mode): 650.8 (calc. 650.6, C28H37N5O11P1). tR= 5.54 (HPLC system A). Example 77: 3.4-Dihydroxvphenvl-acetvl-Tvr(PO..Hp)-lle-Asn-NHρ (SEQ ID NO: 77) 3,4-Dihydroxyphenyl-acetic acid is from Fluka, Buchs, Switzerland and is incorporated with benzotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxy- benzotriazole (1 :1 ; 3 equiv.; first coupling) and N-[(dimethylamino)-1 H-1 ,2,3-triazolo[4,5- b]pyridin-1-ylmethylene]-N-methylmethanaminium hexafluorophosphate N-oxide (3 equiv.; second coupling) in the presence of diisopropylethylamine (7 equiv.). The manual synthesis results in the title compound: Mass-spectral analysis (negative-ion mode): 636.4 (calc. 636.6, C27H35N5O11 P1). tR= 5.43 (HPLC system A). Example 78: trans-3.4-Dihydroxy-cinnamoyl-Tyr(POr.Hp)-Glv-NHp (SEQ ID NO: 78) Mass-spectral analysis (negative-ion mode): 478.4 (calc. 478.4, C20H21N3O9P1). tR= 4.61 (HPLC system A). Example 79: trans-3.4-Dihvdroxy-cinnamoyl-Tvr(POgHp)-βAla-NHp (SEQ ID NO: 79) Mass-spectral analysis (negative-ion mode): 494.4 (calc. 492.4, C21H23N3O9P1). tR= 4.74 (HPLC system A). Example 80: trans-3,4-Dihvdroxv-cinnamovl-Tyr(PO..Hp)-Ac7C-Asn-NHp (SEQ ID NO: 80) Mass-spectral analysis (negative-ion mode): 674.6 (calc. 674.6, C30H37N5O11 P1). tR= 6.03 (HPLC system A). The starting material is prepared as follows: a) Fmoc-1-amino-cvcloheptanecarboxylic acid The title compound is synthesized starting from 1 -amino-cydoheptanecarboxylic acid (see N. Zelinsky and G. Stadnikoff, Chem. Ber., 39, 1722-1732, (1906)) according to a proce¬ dure known in the art (see E. Atherton and R.C. Sheppard, in Solid-Phase Peptide Synthe¬ sis- A Practical Approach, eds.: D. Rickwood and B.D. Hames, IRL Press at Oxford Univer¬ sity Press, Oxford, 1989): R f = 0.25 (dichloromethane:methanol, 9:1 , v/v). Example 81 : trans-3.4-Dihvdroxv-cinnamovl-Tvr(PO.^Hρ)-Nbo-Asn-NHp (SEQ ID NO: 81) Fmoc-2-amino-2-norbornanecarboxyiic acid (2 equiv.) is incorporated with benzotriazole-1- yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxybenzotriazole (1 :1; 2 equiv.) in the presence of diisopropylethylamine (4 equiv.). The manual synthesis yields the title compound: Mass-spectral analysis (negative-ion mode): 672.4 (calc. 672.6, C30H35N5O11 P1). tR= 5.80 (HPLC system A). The starting material is prepared as follows: a) Fmoc-2-amino-2-norbornanecarboxylic acid The title compound is synthesized starting from 2-amino-2-norbornanecarboxylic acid (Aldrich, Buchs, Switzerland) according to a procedure known in the art (see E. Atherton and R.C. Sheppard, in Solid-Phase Peptide Synthesis- A Practical Approach, eds.: D. Rickwood and B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989): Rf= 0.51 (chloroform:methanol:water:acetic acid, 850:130:15:5, v/v/v/v). Example 82: trans-3.4-Dihvdroxv-cinnamovl-Tyr(P03Hp)-Nbo-NH2 (epimer 1) (SEQ ID NO: 82) Fmoc-2-amino-2-norbornanecarboxylic acid (2 equiv.) is incorporated with benzotriazole-1- yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxybenzotriazole (1 :1 ; 2 equiv., first coupling) and N-[(dimethylamino)-1 H-1 ,2,3-triazoio[4,5-b]pyridin-1-ylmethyle- ne]-N-methylmethanaminium hexafluorophosphate N-oxide (2 equiv.; second coupling) in - 88 - the presence of diisopropylethylamine (6 equiv.). Title compound: Mass-spectral analysis (negative-ion mode): 558.7 (calc. 558.5, C26H29N3O9P1). tR= 6.18 (HPLC system A). Example 83: trans-3,4-Dihydroxy-cinnamoyl-Tyr(Pθ3H2)-Nbo-NH2 (epimer 2) (SEQ ID NO: 83) Fmoc-2-amino-2-norbornanecarboxylic acid (2 equiv.) is incorporated with benzotriazole-1- yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxybenzotriazole (1 :1 ; 2 equiv., first coupling) and N-[(dimethylamino)-1 H-1 ,2,3-triazolo[4,5-b]pyridin-1 -ylmethyle- ne]-N-methylmethanaminium hexafluorophosphate N-oxide (2 equiv.; second coupling) in the presence of diisopropylethylamine (6 equiv.). Title compound: Mass-spectral analysis (negative-ion mode): 558.7 (calc. 558.5, C26H29N3O9P1). tR= 6.21 (HPLC system A). Example 84: trans-4-Hydroxy-cinnamoyl-Tyr(PO:-.Hg)-lle-Asn-NHp (SEQ ID NO: 84) trans-4-Hydroxy-cinnamic acid is from Fluka, Buchs, Switzerland and is incorporated (2 equiv.; double coupling) with benzotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexa- fluorophosphate/N-hydroxybenzotriazole (1 :1; 2 equiv.) in the presence of diisopropylethyl¬ amine (4 equiv.). The manual synthesis yields the title compound: Mass-spectral analysis (negative-ion mode): 632.9 (calc. 632.6, C28H35N5O10P1). tR= 6.11 (HPLC system A). Example 85: 6-Hydroxv-2-naphthovl-Tvr(PO'-.Hp)-lle-NHp (SEQ ID NO: 85) 6-Hydroxy-2-naphthoic acid is from Lancaster, Strasbourg, France and is incorporated (2 equiv.; double coupling) with benzotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexa- fluorophosphate/N-hydroxybenzotriazole (1 :1 ; 2 equiv.) in the presence of diisopropylethyl¬ amine (4 equiv.). The manual synthesis results in the title compound: Mass-spectral analy¬ sis (negative-ion mode): 542.2 (calc. 542.5, C26H29N3O8P1). tR= 7.23 (HPLC system A). Example 86: trans-3.4-Dihydroxv-cinnamoyl-Tyr(PQ3Hp)-Gln-NHp (SEQ ID NO: 86) The manual synthesis results in the tilte compound: Mass-spectral analysis (negative-ion mode): 549.4 (calc. 549.5, C23H26N4O10P1). tR= 4.74 (HPLC system A). Example 87: trans-3.4-Dihydroxv-cinnamoyl-Tyr(Pθ3Hp)-Glu-NHp (SEQ ID NO: 87) The side chain of the glutamic acid building block is protected with the tert-butyl group. Manual synthesis results in the title compound: Mass-spectral analysis (negative-ion mode): 550.4 (calc. 550.5, C23H25N3O11 P1). tR= 4.87 (HPLC system A). Example 88: trans-3,4-Dihydroxv-cinnamoyl-Tyr(PO.-.Hp)-Glu-DHph-NH? (SEQ ID NO: 88) N -Fmoc-Z homophenylalanine (2 equiv.; double coupling) is incorporated with 2-(2-pyri- don-1-yl)-1 ,1 ,3,3-tetramethyluronium-tetrafluoroborate (2 equiv.) in the presence of diiso¬ propylethylamine (2.2 equiv.). The side chain of the glutamic acid building block is protected with the tert-butyl group. The manual synthesis results in the title compound: Mass-spectral analysis (negative-ion mode): 711.8 (calc. 711.7, C33H36N4O12P1). tR= 7.40 (HPLC system A). The starting material is prepared as follows: a) N α -Fmoc-D-homophenylalanine The title compound is synthesized starting from D-homophenylalanine (Bachem, Bubendorf, Switzerland) according to a procedure known in the art (see E. Atherton and R.C. Sheppard in Solid-Phase Peptide Synthesis- A Practical Approach, eds.: D. Rickwood and B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989): Rf= 0.44 (dichlorometha- ne:methanol:water:acetic acid, 850:130:15:5, v/v/v/v). Example 89: trans-3.4-Dihydroxy-cinnamovl-Tyr(PO..Hρ)-DHph-NHρ (SEQ ID NO: 89) N α -Fmoc-D-homophenylalanine (2 equiv.) is incorporated with 2-(2-pyridon-1-yl)-1 ,1 ,3,3- tetramethyluroniumtetrafluoroborate (2 equiv.) in the presence of diisopropylethylamine (2.2 equiv.). Mass-spectral analysis (negative-ion mode): 582.7 (calc. 582.5, C28H30N3O9P1). t R = 7.04 (HPLC system A). Example 90: trans-3.4-Dihydroxv-cinnamovl-Tvr(POr.Hp)-Ac5C-NHp (SEQ ID NO: 90) Fmoc-1-amino-cyclopentanecarboxylic acid (2 equiv.) is incorporated with benzotriazole- 1 - yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxybenzotriazole (1 :1 ; 2 equiv.; first coupling) and N-[(dimethylamino)-1 H-1 ,2,3-triazolo[4,5-b]pyridin-1-ylmethyle- ne]-N-methylmethanaminium hexafluorophosphate N-oxide (2 equiv.; second coupling) in the presence of diisopropylethylamine (6 equiv.). The title compound is obtained after manual synthesis: Mass-spectral analysis (negative-ion mode): 532.6 (calc. 532.5, C24H27N3O9P1). tR= 5.41 (HPLC system A). The starting material is obtained as follows: a) Fmoc-1-amino-cvclopentanecarboxylic acid The title compound is synthesized from 1-amino-1 -cyclopentanecarboxylic acid (Aldrich, Buchs, Switzerland) according to a procedure known in the art (see E. Atherton and R.C. Sheppard, in Solid-Phase Peptide Synthesis- A Practical Approach, eds.: D. Rickwood and B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989): Rf= 0.79 (chloroform:methanol:water:acetic acid, 750:270:50:5, v/v/v/v). Example 91 : trans-3,4-Dihydroxv-cinnamovl-Tvr(Pθ3Hp)-Pro-NHp (SEQ ID NO: 91) The manual synthesis results in the titie compound: Mass-spectral analysis (negative-ion mode): 518.6 (calc. 518.5, C23H25N309PT). T.R= 5.22 (HPLC system A). Example 92: 2-Naphthovl-Tvr(PO^Hp)-lle-Asn-NHp (SEQ ID NO: 92) Mass-spectral analysis (negative-ion mode): 640.5 (calc. 640.6, C30H35N5O9P1). tR= 8.05 (HPLC system A). 2-Naphthoic acid is from Fluka, Buchs, Switzerland, and is incorporated (2 equiv.) with ben- zotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxybenzo- triazole (1 :1 ; 2 equiv.; double coupling) in the presence of diisopropylethylamine (4 equiv.). Example 93: 1 -Adamantoyl-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 93) Mass-spectral analysis (negative-ion mode): 648.3 (calc. 648.7, C30H43N5O9P1). tR= 8.23 (HPLC system A). 1-Adamantoic acid is from Fluka, Buchs, Switzerland, and is incorporated (2 equiv.) with benzotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxy- benzotriazole (1 :1 ; 2 equiv.; double coupling) in the presence of diisopropylethylamine (4 equiv.). Example 94: Cvclohexanoyl-Tvr(POr-:Hp)-lle-Asn-NHp (SEQ ID NO: 94) Mass-spectral analysis (negative-ion mode): 596.7 (calc. 596.6, C26H39N5θgPi)- tR= 6.94 (HPLC system A). Cyclohexanoic acid is from Fluka, Buchs, Switzerland, and is incorporated (2 equiv.) with benzotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxy- benzotriazole (1 :1 ; 2 equiv.; double coupling) in the presence of diisopropylethylamine (4 equiv.). Example 95: 3-Cvclohexvl-propionyl-Tvr(POr.Hρ)-lle-NHp (SEQ ID NO: 95) Mass-spectral analysis (negative-ion mode): 510.5 (calc. 510.6, C24H37N3O7P1). tR= 9.17 (HPLC system A). 3-Cyclohexyl-propionic acid is from Fluka, Buchs, Switzerland, and is incorporated (2 equiv.) with benzotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydro- xybenzotriazole (1 :1 ; 2 equiv.; double coupling) in the presence of diisopropylethylamine (4 equiv.). Example 96: 1 ,2,3,4-Tetrahydro-2-naphthoyl-Tyr(PO3H2)-He-NH2 (SEQ ID NO: 96) Mass-spectral analysis (negative-ion mode): 530.6 (calc. 530.6, C26H33N3O7P1). tR= 8.73 (HPLC system A). 1 ,2,3,4-Tetrahydro-2-naphthoic acid is from Fluka, Buchs, Switzerland, and is incorporated (2 equiv.) with benzotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophos- phate/N-hydroxybenzotriazole (1 :1 ; 2 equiv.; double coupling) in the presence of diisopro¬ pylethylamine (4 equiv.). Example 97: Cvclohexanovl-Tvr(POr-:Hp)-lle-NHp (SEQ ID NO: 97) Mass-spectral analysis (negative-ion mode): 482.4 (calc. 482.5, C22H33N3O7P1). tR= 7.65 (HPLC system A). Cyclohexanoic acid is from Fluka, Buchs, Switzerland, and is incorporated (2 equiv.) with benzotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxy- benzotriazole (1 :1 ; 2 equiv.; double coupling) in the presence of diisopropylethylamine (4 equiv.). Example 98: 2-Naphthoyl-Tyr(Pθ3H )-He-NH2 (SEQ ID NO: 98) Mass-spectral analysis (negative-ion mode): 526.6 (calc. 526.5, C26H29N3O7P1). tR= 8.67 (HPLC system A). 2-Naphthoic acid is from Fluka, Buchs, Switzerland and is incorporated (2 equiv.) with ben- zotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxybenzo- triazole (1 :1 ; 2 equiv.; double coupling) in the presence of diisopropylethylamine (4 equiv.). Example 99: 1 -Adamantoyl-Tyr(Pθ3H2)-He-NH2 (SEQ ID NO: 99) Mass-spectral analysis (negative-ion mode): 534.7 (calc. 534.6, C26H37N3O7P1). tR= 9.15 (HPLC system A). 1 -Adamantoic acid is from Fluka, Buchs, Switzerland and is incorporated (2 equiv.) with benzotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxy- benzotriazole (1 :1 ; 2 equiv.; double coupling) in the presence of diisopropylethylamine (4 equiv.). Example 100: 4-Acetamino-benzovl-Tyr(Pθ3Hp)-lle-NHρ (SEQ ID NO: 100) Mass-spectral analysis (negative-ion mode): 533.5 (calc. 533.5, C24H30N4O8P1). tR= 5.99 (HPLC system A). 4-Acetamino-benzoic acid is from Fluka, Buchs, Switzerland and is incorporated (2 equiv.) with benzotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydro- xybenzotriazole (1 :1 ; 2 equiv.; double coupling) in the presence of diisopropylethylamine (4 equiv.). Example 101: Succinamoyl-TvrfPOsHpl-lle-Asn-NHp (SEQ ID NO: 101) Mass-spectral analysis (negative-ion mode): 585.5 (calc. 585.5, C23H34NβOιoPi)- tR= 4.55 (HPLC system A). Succinamic acid is from Aldrich, Buchs, Switzerland, and is incorporated (2 equiv.) with ben- zotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxybenzo- triazole (1 :1 ; 2 equiv.; double coupling) in the presence of diisopropylethylamine (4 equiv.). Example 102: 1 ,2,3,4-Tetrahydro-2-naphthoyl-Tyr(PO3H2)-He-Asn-NH2 (SEQ ID NO: 102) Mass-spectral analysis (negative-ion mode): 644.7 (calc. 644.7, C30H39N5O9P-1). tR= 8.19 (HPLC system A). 1 ,2,3,4-Tetrahydro-2-naphthoic acid is from Fluka, Buchs, Switzerland, and is incorporated (2 equiv.) with benzotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophospha- 93 te/N-hydroxybenzotriazole (1 :1 ; 2 equiv.; double coupling) in the presence of diisopropyl¬ ethylamine (4 equiv.). Example 103: 1 ,2,3,4-Tetrahydro-2-naphthoyl-Tyr(Pθ3H2)-lle-lle-Pro-NH2 (SEQ ID NO: 103) Mass-spectral analysis (negative-ion mode): 740.7 (calc 740.8, C37H51N5O9P1). tR= 6.77 (HPLC system A). 1 ,2,3,4-Tetrahydro-2-naphthoic acid is from Fluka, Buchs, Switzerland, and is incorporated (2 equiv.) with benzotriazole-1 -yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophospha- te/N-hydroxybenzotriazole (1 :1 ; 2 equiv.; double coupling) in the presence of diisopropyl¬ ethylamine (4 equiv.). Example 104: trans-3,4-Dihydroxy-cinnamovl-Tyr(Pθ3Hp)-Hph-NH2 (SEQ ID NO: 104) Mass-spectral analysis (negative-ion mode): 582.5 (calc. 582.5, C28H29N3O9P1). tR= 6.92 (HPLC system A). The starting material is prepared as follows: a) Fmoc-L-homo-phenylalanine The title compound is synthesized starting from L-homophenylalanine (H-Hph-OH, Bachem, Bubendorf, Switzerland) according to a procedure known in the art (see E. Atherton and R.C. Sheppard, in Solid-Phase Peptide Synthesis- A Practical Approach, eds.: D. Rickwood and B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989): Rf= 0.63 (chloro- form:methanol:water:acetic acid, 750:270:50:5). Example 105: trans-3.4-Dihydroxy-cinnamovl-Tyr(P03Hp)-lle-Asn-NH2 (SEQ ID NO: 105) The peptide is synthesized on a Milligen 9050 automated peptide synthesizer (continuous flow; Millipore, Bedford, MA, USA), starting with an Fmoc-PAL-PEG-PS resin (see Albericio, F. et al. J. Org. Chem., 55 (1990) 3730-3743) for establishing the C-terminal caboxamide, and using chemical protocols based on the fluorenylmethoxycarbonyl chemistry (see E. Atherton and R.C. Sheppard, in Solid-Phase Peptide Synthesis- A Practical Approach, eds.: D. Rickwood and B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989). The required Fmoc-amino acids (3 equiv.) are coupled using their 2,4,5-trichlorophenyl esters (single coupling) with minimum reaction times of 30 min (see 9050 Plus PeptSynthesizer, User's Guide, Millipore Corporation, Bedford, MA, 1992). The incorporation of N α -Fmoc- Tyr(P0 3 H 2 )-OH (3 equiv.) and trans-3,4-dihydroxy-cinnamic acid are accomplished with benzotriazole-1-yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophosphate/N-hydroxy- benzotriazole (1 :1 ; 3 equiv., first coupling) and N-[(dimethylamino)-1 H-1 ,2,3-triazolo[4,5- b]pyridin-1-ylmethylene]-N-methylmethanaminium hexafluorophosphate N-oxide (3 equiv.; second coupling) in the presence of diisopropylethylamine (6 equiv.). The complete peptide resin obtained after the last coupling step is simultaneously deprotected and cleaved by treatment with trifluoroacetic acid/H 2 O (95:5, v/v) for 3 h at room temperature. The filtrate from the cleavage reaction is precipitated in diisopropyl ether/petroleum ether (1 :1 , v/v, 0 °C), and the precipitate collected by filtration. The crude peptide is purified by medium- pressure liquid chromatography as described in -Example 1. Title compound: Mass-spectral analysis (negative-ion mode): 648.3 (calc. 648.6, C28H35N5O11 P1). tR= 5.88 (HPLC system A). Example 106: trans-3.4-Dihvdroxv-cinnamoyl-Tvr(PO^Hp)-lle-βAla-NHρ (SEQ ID NO: 106) Fmoc-β-alanine is from Novabiochem (Laufelfingen, Switzerland) and is incorporated (3 equiv.) with benzotriazole-1 -yl-oxy-tris-dimethylamino)-phosphoniumhexafluorophospha- te/N-hydroxybenzotriazole (1 :1 ; 3 equiv.) in the presence of diisopropylethylamine (6 equiv.). Title compound: Mass-spectral analysis (negative-ion mode): 605.6 (calc. 605.6, C26H34N4O10P1). tR= 5.85 (HPLC system A). Example 107: trans-3.4-Dihvdroxv-cinnamovl-Tvr(Pθ3Hp)-lle-Gln-NHp (SEQ ID NO: 107) Automatic synthesis yields the title compound: Mass-spectral analysis (negative-ion mode): 661.0 (calc. 662.6, C29H37N5O11 P-|). tR= 5.87 (HPLC system A). Example 108: trans-3.4-Dihvdroxv-cinnamoyl-Tvr(Pθ3Hp)-lle-Gly-NHp (SEQ ID NO: 108) Automatic synthesis yields the title compound: Mass-spectral analysis (negative-ion mode): 591.1 (calc. 591.5, C26H32N4O10P1). tR= 6.18 (HPLC system A). Example 109: trans-3,4-dihvdroxv-cinnamovl-F ? Pmp-lle-Asn-NHp (SEQ ID NO: 109) The peptide is synthesized manually on a 4-(2',4'-dimethoxyphenyl-aminomethyl)-phenoxy resin, employing a procedure analogous to Example 67. Incorporation of N α -Fmoc-[4-(O- diethyl)-phophono(difluoromethyl)]-L-phenylalanine (for synthesis see Tetrahedron Lett. 34 (22), 3543 (1993)) to the protected peptide resin is carried out with benzotriazole-1yl-N- oxytris-(dimethylamino)-phosphonium hexafluorophosphate/N-hxdroxybenzotriazole (1:1 , 3 equiv.) in the presence of diisopropylethylamine (7 equiv.), 3 h reaction time, trans-3,4- Dihydroxy-cinnamic acid (3 equiv.) is incorporated with benzotriazole-1-yl-oxy-tris-dimethyl- amino)-phosphoniumhexafluorophosphate/N-hydroxybenzotriazole (1:1 ; 3 equiv., first coupling) in the presence of diisopropylethylamine (7 equiv.), 2 h reaction time. The complete peptide resin obtained after the last coupling step is deprotected and cleaved via a two step process. The peptide is removed from the solid-support and partially deprotected by treatment with trifluoroacetic acid/H 2 O (95:5, v/v) for 3 h at room temperature. The cleavage of the phosphonate diester protecting groups is carried out as follows: The crude compound is suspended in MeCN (1 ml) and trimethylsilyl-iodide (1 ml) is added dropwise to the suspension. The course of the reaction is followed by analytical HPLC. After 60 min complete reaction is achieved. Reaction is terminated by removal of MeCN followed by addition of a 10 % solution of aqueous AcOH (12 ml) to hydrolyze the trimetylsilyl ester in¬ termediates. The aqueous solution is extracted with diethylether, concentrated and injected directly in the medium-pressure liquid chromatography system (see Example 1). Title com¬ pound: Mass-spectral analysis (negative-ion mode): 682.8 (calc. 682.6, C29H35N5O-10F2P1). tR= 5.65 (HPLC system A). Example 110: trans-3.4-Dihydroxv-cinnamovl-FpPmp-lle-NHp (SEQ ID NO: 110) Manual synthesis results in the title compound: Mass-spectral analysis (negative-ion mode): 568.2 (calc. 568.5, C25H29N3O8F2P1). tR= 6.63 (HPLC system A). Example 111 : 3-Aminobenzyloxycarbonyl-Tyr(Pθ3H2)-Met-Asn-NH2 (TFA salt) (SEQ ID NO: 111) By manual synthesis, the title compound is obtained in analogy to Example 3: Mass spectral analysis (negative-ion mode): 653.7 (calc. 653.6, C26H34N6O10P1S1), tR= 4.88 min (HPLC System A). Example 112: lndole-5-ylcarbonyl-Tyr-lle-Asn-Gln-NH2 (SEQ ID NO: 112) In analogy to Example 61 , the title compound is obtained by manual synthesis: Mass spectral analysis (negative-ion mode): 677.8 (calc. 677.7, C33H41 N8O8), tR= 7.12 min (HPLC System A). Example 113: Cyclohexanecarbonyl-Tyr(Pθ3Hp)-He-Asn-NH2 (SEQ ID NO: 113) Cyclohexanecarboxylic acid (2 equiv.; Fluka, Buchs, Switzerland) is coupled with BOP/HOBt (1 :1 , 2 equiv.) in the presence of diisopropylethylamine (4 equiv.) in N-methylpyrrolidin-2- one, yielding the title compound: Mass spectral analysis (negative-ion mode): 596.7 (calc 596.6, C26H39N5O9P1), tR= 6.94 min (HPLC System A). Example 114: 2-Naphthvlcarbonvl-Tyr(Pθ3Hp)-lle-Asn-NHp (SEQ ID NO: 114) 2-Naphthoic acid (2 equiv.; Fluka, Buchs, Switzerland) is coupled with BOP/HOBt (1 :1 , 2 equiv.) in the presence of diisopropylethylamine (4 equiv.) in N-methylpyrrolidin-2-one, yiel¬ ding the title compound: Mass spectral analysis (negative-ion mode): 640.5 (calc. 640.6, C30H35N5O9P1), tR= 8.05 min (HPLC System A). Example 115: lndole-5-ylcarbonvl-L-FpPmp-lle-Asn-NHp (SEQ ID NO: 115) In analogy to example 64, the title compound is obtained by manual synthesis: Mass spectral analysis (negative-ion mode): 663.7 (calc. 663.6, C29H34N6O8P1 F2), tR= 6.63 min (HPLC System A). Example 116: 9-Fluorenvlcarbonvl-Tvr(PO.3Hp)-lle-Asn-NHp (SEQ ID NO: 116) The synthesis proceeds manually. 9-Fluorenecarboxylic acid (3 equiv.; Aldrich, Steinheim, Germany) is coupled with BOP/HOBt (1 :1 , 3 equiv.; first coupling) and HATU (3 equiv.; second coupling) in the presence of diisopropylethylamine (7 equiv.) in N-methylpyrrolidin-2- one, yielding the title compound: Mass spectral analysis (negative-ion mode): 678.5 (calc 678.7, C33H37N5O9P1), tR= 8.01 min (HPLC System A). Example 117: 3-Aminobenzyloxycarbonyl-Tyr(Pθ3H2)-Gln-Asn-NH2 (TFA salt) (SEQ ID NO: 117) Manual synthesis yields the title compound: Mass spectral analysis (negative-ion mode): 650.7 (calc. 650.6, C26H33N7O11 P-|), tR= 3.78 min (HPLC System A). Example 118: 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-Tle-Asn-NH2 (TFA salt) (SEQ ID NO: 118) Synthesis is manually. N α -Fmoc-L-α-t-butyl-glycine (2 equiv.; Novabiochem, Laufelfingen, Switzerland) is coupled with BOP/HOBt (1 :1 , 2 equiv.) in the presence of diisopropylethyl- amine (5 equiv.) in N-methyipyrrolidin-2-one. Title compound: Mass spectral analysis (nega¬ tive-ion mode): 635.3 (calc. 635.6, C27H36N6O10P1), tR= 5.53 min (HPLC System A). Example 119: 3-Aminobenzyloxycarbonyl-L-Pmp-lle-Asn-NH2 (TFA) (SEQ ID NO: 119) Synthesis is manually. N- α -Fmoc-p-(bisethoxyphosphoryl-methyl)-Phe-OH (1.5 equiv.; Neosystem Catalogue; See also C. Garbay-Jaureguiberry et al., Int. J. Pept. Prot. Res. 39, 523-527 (1992)) is incorporated with BOP/HOBt 1 :1 ; 1.5 equiv.) in the presence of diisopro¬ pylethylamine (4 equiv.) in N-methylpyrrolidin-2-one. After the addition of the building block, the Fmoc group is removed and the peptide resin is cleaved with trifluoroacetic acid/water (95:5, v/v, v/v) for 3 h at room temperature. The filtrate is precipitated in diisopropyl ether- petroleum ether (1 :1 , v/v) at 0 °C, and the precipitate is collected by filtration. The com¬ pound (68 mg) is dissolved in acetonitrile (2 ml) and trimethylsilyl iodide (1.7 ml; Fluka, Buchs, Switzerland) is added. The course of the reaction is monitored by analytical HPLC using a reversed-phase column. After 1.5 h at room temperature, the solution is concentra¬ ted to dryness and the crude compound is dissolved in 10% AcOH in water (5 ml). The so¬ lution is extracted with ether (x2) and the aqueous phase is injected directly to the medium- pressure liquid chromatography system decribed in Example 1 , yielding the title compound: Mass spectral analysis (negative-ion mode): 633.5 (calc. 633.6, C28H38N6O9P1), tR= 5.44 min (HPLC System A). Example 120: 3-Aminobenzyloxycarbonyl-Tyr(Pθ3H2)-Ac6C-Asn-NH2 (TFA salt) (SEQ ID NO: 120) Manual synthesis results in the title compound: Mass spectral analysis (negative-ion mode): 647.7 (calc. 647.6, C28H36N6O10P1), tR= 5.38 min (HPLC System A). Example 121 : Acetyl-Tyr(PO3H )-lle-Asn-NH-(3-naphthalen-1 -yl-propyi) (SEQ ID NO: 121) The peptide is synthesized manually on a 4-(2',4',-dimethoxyphenyl-Fmoc-aminomethyl)- phenoxyacetamido-norleucyl-MBHA resin (commercially available from Novabiochem, Laufelfingen, Switzerland, 0.55 mmol/g), employing the Fmoc strategy (see E.Atherton and R.C.Sheppard, in Solid-Phase Peptide Synthesis- A Practical Approach, ed. D.Rickwood and B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989). Fmoc is removed with piperidine/ dimethylacetamide (1 :4, v/v; 6 x 2 min) followed by washing with isopropa¬ nol (3 x 1 min), dimethylacetamide (2 x 1 min), isopropanol (3 x1 min) and dimethylacet¬ amide (2 x 1 min). Coupling is achieved by first dissolving the Fmoc-amino acid (3 equiv.) , diisopropylethyl amin (3.3 equiv.), and the 2-(2-pyridon-1 -yl)-1 ,1 ,3,3-tetramethyluroniumte- trafluoroborate reagent (TPTU, commercially available from Senn Chemicals, Dielsdorf, Switzerland; 3 equiv.) in N-methylpyrrolidin-2-one, then waiting 3 min for preactivation, ad¬ ding the mixture to the resin, and finally shaking for at least 45 min. N α -Fmoc-aspartic acid α-allylic ester (Novabiochem, Laufelfingen, Switzerland) is coupled through its side chain to the resin. The incorporation of N α -Fmoc-Tyr(PO 3 H)-OH (see Biochemistry 32, 4354 (1993) (3 equiv.) is accomplished with BOP/ HOBt (1 :1 ; 2 equiv.; first coupling) in the presence of diisopropylethylamine (6 equiv.) and N-[(dimethylamino)-1 H-1 ,2,3-triazolo[4,5-b]pyridin-1- ylmethylene]-N-methylmethanaminium hexafluorophosphate N-oxide (HATU, 2 equiv., second coupling) in the presence of diisopropylethylamine (6 equiv.). Acetylation is perfor¬ med with acetic anhydride and pyridine in dimethylacetamide (1 :1 :8 v/v) for 2 min followed by washing with dimethylacetamide and dichloromethane. For the removal of the α-allyl ester group, the dried peptide resin is re-suspended in a degassed solution of acetic acid and N-methylmorpholin in chloroform (2:1 :37 v/v) followed by addition of tetrakis- (triphenyl¬ phosphine)- palladium(O) (0.8 equiv.) under an argon atmosphere (see F. Albericio, G. Barany, G.B. Fields, D. Hudson, S.A. Kates, M.H. Lyttle, N.A. Sole, in Peptides 1992, CH. Schneider, A.N. Eberle (eds), ESCOM, Leiden, 1993, p.191 ; S.A. Kates, S.B. Daniels, N.A. Sole, G. Barany, F. Albericio, in Peptides; Chemistry & Structure, R.S. Hodges, J.A. Smith (eds), ESCOM, Leiden, 1994, p.113). After treatment for 3h, the resin is washed with chlo¬ roform (3 x 1 min) , dimethylformamide (3 x 1min), a solution of sodium diethyldithiocarba- mate (0.05M) containing 0.5% diisopropylethylamine in dimethylformamide (2 x 1 min), di¬ methylformamide (2 x 1 min) and dichloromethane (3 x1 min) and dried. The final incorpo¬ ration of 3-naphthalen-1 -yl-propylamine (4 equiv.) is accomplished with TPTU/ HOBt (1 :1 , 6 equiv.) in the presence of diisopropylethylamine (9 equiv.) with N-methylpyrrolidin-2-one as solvent. The complete peptide resin obtained after the final washing steps with dimetylacet- amide (2 x 1min), isopropanol (2 x 1 min) dimetylacetamide (2x1 min), dichloromethane (3 x 1 min) is simultaneously deprotected and cleaved by treatment with trifluoroacetic acid/ H2O (95:5, v/v) for 3 h at room temperature. The filtrate from the cleavage reaction is preci¬ pitated in tert-butyl-methyl ether/petroleum ether (1 :1 , v/v, 0 °C), and the precipitate is col¬ lected by centrifugation. The crude peptide is purified by medium-pressure liquid chromato¬ graphy using a C 18 reversed phase column (Merck © LICHROPREP RP-18, 15-25 μm bead diameter, reversed phase HPLC column material based on C-| s-derivatized silicagel, Merck, Darmstadt, FRG; column length 46 cm, diameter 3.6 cm; flow rate 53.3 ml/min; detection at 215nm), eluted with an acetonitriie-water gradient containing 0.1% of TFA. The title com¬ pound is obtained: Mass spectral analysis (matrix-assisted laser-desorption ionisation time- of-flight mass spectrometry, MALDI-TOF and fast atom bombardment mass spectroscopy, FAB) reveals a molecular mass within 0.1% of the expected values (negative- ion mode: 696.0 [M-H]+, (C34H44N5O9P: 697.73)). The purity of the peptide is verified by reversed- phase analytical HPLC on a Nudeosil C-| Q column (250x4 mm, 5 μm (AB), 10θA, from Macherey-Nagel): linear gradient of acetonitrile/ 0.09% TFA and H2O/ 0.1 % TFA from 1 :49 to 3:2 over 10 min; flow rate 1.5 ml/min, detection at 215 nm; single peak at t = 8.56 min (HPLC System D). The starting material is obtained as follows: a) 3-(1-Naphthyl)-acrylonitril A mixture of 6.8 ml (7.8 g = 0.05 mol) 1 -naphthaldehyd (Aldrich, Buchs, Switzerland) and 7.9 ml (8.8 g = 0.05 mol) diethyl cyanomethylphosphonate (Fluka, Buchs, Switzerland) is treated dropwise with 17 ml of a 6 molar potassium carbonate solution (0.1 mol) under stirring. The temperature is kept at 20°C by cooling in an ice bath. After complete addition, the mixture is stirred 10 minutes at room temperature. Thin layer chromatography (tolu¬ ene/ethyl acetate 1 :1) indicates the end of the reaction. After dilution with ethyl acetate, the reaction mixture is washed with water, dried over sodium sulfate, filtered and evaporated. The residue, a viscous oil, is purified by flash-chromatography (toluene/petrol ether 1:1). The title compound is obtained as a colorless oil. Rf (toluene/petrol ether 1 :1) = 0.15 b) 3-(1 -Naphthyl)-1 -propylamine hydrochloride 6.8 g (0.0379 mol) of 3-(1 -naphthyl)-acrylonitril are hydrogenated at normal pressure and at 45°C in presence of 2.0 g of Raney-Nickel (Fluka, Buchs, Switzerland) in 220 ml methanol containing 5 % ammonia. The catalyst is removed by filtration, and the methanol is evapo¬ rated. The residue is purified by flashchromatography (ethyl acetate/methanol 9:1 contai¬ ning 1% cone ammonia). 3-(1-naphthyl)-1 -propylamine is obtained: Rf (ethyl acetate/ methanol 1 :1 containing 1% cone ammonia) = 0.10 The free base is dissolved in 40 ml of ethanol and treated with 10 ml of a 10% solution of hydrogen chloride in ethanol (approximately 0.03 mol). The solution is concentrated and the product precipitated by addition of ether. The product is collected by filtration, yielding the title compound: Melting point 154-156°C. The following examples 122 to 139 are obtained in analogy to the title compound of Example 121 , if not indicated otherwise: Acetyl-Tyr(PO3H2)-He-Asn-NH-[3-(2-hydroxy-naphthalen-1-yl)-propyl] (SEQ ID NO: 122) 1-(3-Aminopropyl)-naphthol-(2) is synthesized according to known procedures (see H. Plieninger, Chem. Ber. 87, 232 (1954)), starting from 1-(2-cyanoethyl) -naphthol- (2) Title compound: Mass spectral analysis (negative-ion mode): 713.0 [M-H] + , (C34H44N5O10P, calc 713.73), t R = 8.01 min (HPLC System D). Exarnβle_123: Acetyl-Tyr(Pθ3H2)-He-Asn-NH-(3-naphthalen-2-yl-propyl) (SEQ-ID-NO: 123) Title compound: Mass spectral analysis (negative-ion mode): 696.7 [M-H] + , (C34H44N5O9P, calc. 697.73), t R = 8.75 min (HPLC System D). The starting material is obtained as follows: a) 3-(2-Naphthyl)-acrylonitril This product is synthesized as described for 3-(1-naphthyl)-acrylonitril (Example 123 a). Starting from 15.6 g (0.1 mol) 2-naphthaldehyd, of 3-(2-naphthyl)-acrylonitril are obtained as an oil: Rf (toluene/petrol ether 4:1) = 0.30 b) 3-(2-Naphthyl)-1 -propylamine hydrochloride This product is synthesized as described for 3-(1-naphthyl)-1 -propylamine hydrochloride (Example 122 b). Starting from 12.0 g (0.067 mol) 3-(2-naphthyl)-acrylonitril, 3-(2-naphthyl)- 1 -propylamine is obtained: Rf (ethyl acetate/methanol 9:1 containing 1% cone ammonia) = 0.10. This material is converted to the hydrochloride, yielding the title compound: Melting point 250-253°C. Exarnrjle_124: Acetyl-Tyr(Pθ3H2)-He-Asn-NH-(3-phenanthren-9-yl-propyl) (SEQ ID NO: 124) Title compound: Mass spectral analysis (negative-ion mode): 747.0 [M-H] + , ( c 38 H 46 N 5θgP, calc 747.79), t R = 9.43 min (HPLC System D). The starting material is obtained as follows: a) 3-(Phenanthren-9-yl)-propylamine The title compound is synthesized starting with a Grignard reaction between 9- bromophenanthrene (Fluka, Buchs, Switzerland) and ethylene oxide (Fluka, Buchs, Switzerland). The resulting alcohol is converted to the chloride with thionylchloride in the presence of pyridine in chloroform (see D.J. Jakiela, P.Helquist, L.D. Jones, Organic Synthesis 1983, 62, p.74). Then, conversion of the halide to the nitrile is achieved with potassium cyanide and a catalytic amount of sodium iodide in dimethylsulfoxide as solvent (see D.Brett, I.M.Downie, J.B. Lee, J.Org.Chem 1967, 32, p.855). Finally, LiAIH 4 reduction provides 9-phenanthren-9-yl-propylamine. NMR spectra and mass spectra are in agreement with published data (see F.D.Lewis, G.D. Reddy, B.E. Cohen, Tetrahedron Letters 1994, 35, p.535). Example 125: Acetvl-Tvr(Pθ3H2.-He-Asn-NH-[2-(1 -bromo-naphthalen-2-yloxv)-ethvll (SEQ ID NO: 125) Title compound: Mass spectral analysis (negative-ion mode): 777.3 [M-H] + , ( C 33 H 41 Bi"N 5 O 10 P, calc. 778.60), t R = 8.79 min (HPLC System D). The starting material is obtained as follows: a) (1-Bromo-naphthalen-2-yloxy)-acetonitrile To a stirred mixture containing 1-Brom-2-naphthol (44.6g, 0.2 mol, Aldrich, Buchs, Switzer¬ land), potassium carbonate (30.5g, 0.22 mol) and potassium iodide (10g) in methyl-ethyl- ketone chloroacetonitrile is added at 60 °C. After stirring for 6h at 80 °C, the reaction is cooled to room temperature and then filtered. The filtrate is evaporated to dryness. The residue obtained is partitioned between toluene and water. After separation, the organic layer is washed with 2N NaOH and water, dried and the solvent evaporated. The crude product is dissolved in dichloromethane, purified by filtration through silica gel and crystallized by adding hexane to the solution. Crystalline (1 -bromo-naphthalen-2-yloxy)- acetonitriie is obtained, Rf= 0.37 (ethylacetate/ hexane 1 :3), melting point 96-98 °C. b) 2-(1-Bromo-naphthalen-2-yloxy)-ethylamine hydrochloride To a boiling solution of (1-Bromo-naphthalen-2-yloxy)-acetonitrile (15.72 g, 0.06 mol) in tetrahydrofurane (6ml), borane dimethylsulfide (6.25ml, 0.066 mol) is added dropwise in 20 min. After that, the reaction mixture is kept stirring for additional 20 min at 80 °C. After cooling to room temperature, 1 M methanolic HCI (70 ml) is slowly added, and the hydrolysis is completed by refluxing the mixture for 5h. The volatile components are removed by distil¬ lation, and the residue is treated with methanol. After evaporating the solvent, the crude product is dissolved in boiling ethanol, filtered and crystallized by adding diethyl ether to result in 2-(1 -bromo-naphthalen-2-yloxy)-ethylamine hydrochloride, obtained as yellowish crystals, m.p. 265 °C (decomposition). Example 126: Acetvl-Tvr(Pθ3Hp)-lle-Asn-NH-.3.3-diphenvl-propyl) (SEQ ID NO: 126) 3,3-Diphenylpropylamine is from Aldrich, Buchs, Switzerland. Title compound: Mass spectral analysis (negative-ion mode): 722.4 [M-H] + , (C36H46N5O9P, calc 723.77), t R = 8.99 min (HPLC System D). Example 127: Acetvl-Tv POg^ -He-Asn-NH-Q-phenvl-propvl) (SEQ ID NO: 127) 3-Phenylpropylamine is from Fluka, Buchs, Switzerland. Title compound: Mass spectral analysis (negative-ion mode): 647.6 [M-H] + , (C30H42N5O9P, calc. 647.68), t R = 7.62 min (HPLC System D). Exarnrjkιl28: Acetyl-Tyr(Pθ3H2)-He-Asn-NH-[3-(2,4-dichloro-phenyl)-propyl] (SEQ ID NO: 128) 3-(2,4-dichloro-phenyl)-propylamine is from Fluka, Buchs, Switzerland. Title compound: Mass spectral analysis (negative-ion mode): 715.7 [M-H] + , (C30H40CI2N5O9P, calc. 716.56), t R = 8.91 min (HPLC System D). Exanτple_1 9: Acetyl-Tyr(P0 3 H2)-He-Asn-NH-(2,2-diphenyl-ethyl) (SEQ ID NO: 129) 2,2-Diphenylethylamine is from Aldrich, Buchs, Switzerland. Title compound: Mass spectral analysis (negative-ion mode): 709.0 [M-H] + , C35H44N5O9P, calc. 709.74), tR= 8.69 min (HPLC System D). Example 130: Acetyl-Tvr(Pθ3H2^He-Asn-NH-f2-(4-chloro-phenvl)-ethvll (SEQ ID NO: 130) 2-(4-Chloro-phenyl)-ethylamine is from Fluka, Buchs, Switzerland. Title compound: Mass spectral analysis (negative-ion mode): 667.0 [M-H] + , (C29H39CIN5O9P, calc. 668.04), t R = 7.95 min (HPLC System D). Example 131 : Acetvl-Tvn ^^VHe-Asn-NH-benzvl (SEQ IS NO: 131) Benzylamine is from Fluka, Buchs, Switzerland. Title compound: Mass spectral analysis (negative-ion mode): 618.2 [M-H] + , ( C 28 H 38 N 5C-9P. calc. 619.62), t R = 6.69 min (HPLC System D). Example 132: Acetvl-TvrfPO^HpHle-Asn-NH-isobutvl (SEQ ID NO: 132) Isobutylamine is from Fluka, Buchs, Switzerland. Title compound: Mass spectral analysis (negative-ion mode): 584.7 [M-H] + , (C25H40N5O9P, calc. 585.59), tR= 6.27 min (HPLC System D). Examτp!e_133: Acetyl-Tyr(P0 3 H2)-He-Asn-NH-(3-methyl-butyl) (SEQ ID NO: 133) Isopentylamine is from Fluka, Buchs, Switzerland. Title compound: Mass spectral analysis (negative-ion mode): 598.6 [M-H] + , (C26H42 5O9P, calc. 599.62), tR= 6.98 min (HPLC System D). Exaπιpjte_134: Acetyl-Tyr(P0 3 H2)-lle-Asn-NH-(2-ethyl-hexyl) (SEQ ID NO: 134) (±)-2-Ethylhexylamine is from Fluka, Buchs, Switzerland. Title compound: Mass spectral analysis (negative-ion mode): 641.2 [M-H] + , (C29H 4 8N 5 0gP, calc. 641.71), t R = 8.85 min (HPLC System D). Example 135: Acetyl-Tyr(Pθ3H2.-lle-Asn-NH-cvclohexvl (SEQ ID NO: 135) Cyclohexylamine is from Fluka, Buchs, Switzerland. Title compound: Mass spectral analysis (negative-ion mode): 610.3 [M-H] + , (C27H42N5O9P, calc. 611.64), t R = 6.93 min (HPLC System D). Example 136: Acetvl-Tvr(Pθ3H2)-He-Asn-NH-cvclohexvlmethyl (SEQ ID NO: 136) Aminomethyl-cyclohexane is from Fluka, Buchs, Switzerland. Title compound: Mass spectral analysis (negative-ion mode): 624.7 [M-H] + , (C28H44N5O9P, calc. 625.67), t R = 7.62 min (HPLC System D). Example 137: Acetyl-Tyr(Pθ3H2)-Ac6C-Asn-NH-(3-naphthalen-1 -yl-propyl) (SEQ ID NO: 137) The title compound is prepared in analogy to Example 121. Example 138: Acetvl-Tvr(Pθ3H2.-Acgc-Asn-NH-(3-naphthalen-2-vl-propyl) (SEQ ID NO: 138) The title compound is prepared in analogy to Example 123. (SEQ ID NO: 139) The title compound is prepared in analogy to Example 122. Example 140: 3-Aminobenzvloxvcarbonvl-Tvr(Pθ3H2. -He-Asn-NH-(3-naphthalen-1 -vl- propyl) (SEQ ID NO: 140) The peptide is synthesized manually on a 4-(2',4',-dimethoxyphenyi-Fmoc-aminomethyl)- phenoxyacetamido-norleucyl-MBHA resin (commercially available from Novabiochem, Lau¬ felfingen, Switzerland, 0.55 mmol/g), employing the Fmoc strategy (see E.Atherton and R.C. Sheppard, in Solid-Phase Peptide Synthesis- A Practical Approach, ed. D.Rickwood and B.D. Hames, IRL Press at Oxford University Press, Oxford, 1989). Fmoc is removed with piperidine/ dimethylacetamide (1 :4, v/v; 6 x 2 min) followed by washing with isopropa¬ nol (3 x 1 min), dimethylacetamide (2 x 1 min), isopropanol (3 x1 min) and dimethylacet¬ amide (2 x 1 min). Coupling is achieved by first dissolving the Fmoc-amino acid (3 equiv.) , diisopropylethylamine (3.3 equiv.), and the 2-(2-pyridon-1-yl)-1 ,1 ,3,3-tetramethyluroniumte- trafluoroborate reagent (TPTU, commercially available Senn chemicals, Dielsdorf, Switzer¬ land; 3 equiv.) in N-methylpyrrolidin-2-one, then waiting 3 min for preactivation, adding the mixture to the resin, and finally shaking for at least 45 min. N α -Fmoc-asparagine-α-allylic ester (Novabiochem, Laufelfingen, Switzerland) is coupled through its side chain to the resin. The incorporation of N α -Fmoc-Tyr(P0 3 H 2 )-OH (see Biochemistry 32, 4354 (1993) (3 equiv.) is accomplished with BOP/ HOBt (1 :1 ; 2 equiv.; first coupling) in the presence of diisopropylethylamine (6 equiv.) and N-[(dimethylamino)-1 H-1 ,2,3-triazolo[4,5-b]pyridin-1- ylmethylene]-N-methylmethanaminium hexafluorophosphate N-oxide (HATU, 2 equiv., se¬ cond coupling) in the presence of diisopropylethylamine (6 equiv.). 3-N-tert-Butoxy-carbo- nyl-aminobenzyl-4-nitrophenyl-carbonate (3 equiv.) is coupled to the N-terminal residue of the peptide in the presence of an equimolar amount of diisopropylethylamine in N-methyl- pyrrolidin-2-one during 17h at room temperature. For the removal of the α-allylic ester group, and the dried peptide resin is re-suspended in a degassed solution of acetic acid and N-methylmorpholin in chloroform (2:1 :37 v/v) followed by addition of tetrakis- (tripheπyl- phosphne)-palladium(O) (0.8 equiv.) under an argon atmosphere (see F. Albericio, G. Barany, G.B. Fields, D. Hudson, S.A. Kates, M.H. Lyttle, N.A. Sole, in Peptides 1992, c.H. Schneider, A.N. Eberle (eds), ESCOM, Leiden, 1993, p.191 ; S.A. Kates, S.B. Daniels, N.A. Sole, G. Barany, F. Albericio, in Peptides; chemistry & Structure, R.S. Hodges, J.A. Smith (eds), ESCOM, Leiden, 1994, p.113). After treatment for 3h, the resin was washed with chloroform (3 x 1 min) , dimethylformamide (3 x 1 min), a solution of sodium diethyldithio- carbamate (0.05M) containing 0.5% diisopropylethylamine in dimethylformamide (2 x 1 min), dimethylformamide (2 x 1 min) and dichloromethane (3 x1 min) and dried. The final incorporation of 3-naphthalen-1 -yl-propylamine (4 equiv.) is accomplished with TPTU/ HOBt (1 :1 , 6 equiv.) in the presence of diisopropylethylamine (9 equiv.) with N-methylpyrrolidin-2- one as solvent. The complete peptide resin obtained after the final washing steps with dimetylacetamide (2 x 1min), isopropanol (2 x 1 min) dimetylacetamide (2x1 min), di¬ chloromethane (3 x 1 min) is simultaneously deprotected and cleaved by treatment with trifluoroacetic acid/ H2O (95:5, v/v) for 3 h at room temperature. The filtrate from the clea¬ vage reaction is precipitated in tert-butyl-methyl ether/petroleum ether (1 :1 , v/v, 0 °c), and the precipitate is collected by centrifugation. The crude peptide is purified by medium-pres¬ sure liquid chromatography using a C-J S reversed phase column (Merck ® LICHROPREP RP- 18, 15-25 μm bead diameter, reversed phase HPLC column material based on Ci 8-deri- vatized silicagel, Merck, Darmstadt, FRG; column length 46 cm, diameter 3.6 cm; flow rate 53.3 ml/min; detection at 215nm), eluted with an acetonitrile-water gradient containing 0.1% of TFA. The title compound is obtained: Mass spectral analysis (matrix-assisted laser-de- sorption ionisation time-of-flight mass spectrometry, MALDI-TOF and electro-spray ionisa- tion mass spectroscopy, ESI) reveals a molecular mass within 0.1% of the expected values (negative- ion mode: 803.0 [M-H]+, (C40H49N6O10P. calc. 804.85). The purity of the pep ¬ tide is verified by reversed-phase analytical HPLC on a Nudeosil C-| 8-column (250x4 mm, 5 μm (AB), 10θA, from Macherey-Nagel): linear gradient of acetonitrile/ 0.09% TFA and H2O/ 0.1% TFA from 1 :49 to 3:2 over 10 min; flow rate 1.5 ml/min detection at 215 nm; single peak at t R = 8.6 min (HPLC System D). The following examples 141 to 149 are obtained in analogy to the title compound of Example 140 and Examples 121 to 139 where also starting materials are described, if not mentioned otherwise: Example 141 : S-Aminobenzvloxvcarbonvl-Tvr OgHp) -He-Asn-NH-r3-(2-hydroxy- naphthalen-1 -yl)-propyl] (SEQ ID NO: 141) Title compound: Mass spectral analysis (negative-ion mode): 819.7 [M-H] + , ( C 40 H 49 N 6°11 p . calc - 820.84), t R = 8.11 min (HPLC System D). Example 142: 3-Aminobenzvloxvcarbonvl-Tvr(Pθ3Hp)-lle-Asn-NH-(3-naphthalen-2-yl- propyl) (SEQ ID NO: 142) Title compound: Mass spectral analysis (negative-ion mode): 803.7 [M-H] + , ( C 40 H 49 N 6°10 P ' calc - 804.85), t R = 8.81 min (HPLC System D). Example 143: 3-Aminobenzvloxvcarbonvl-Tyr(Pθ3H2.-He-Asn-NH-(3-phenanthren-9-yl- propyl) (SEQ ID NO: 143) Title compound: Mass spectral analysis (negative-ion mode): 853.2 [M-H] + , (C 4 4H 5 ι 6 Oι 0 P, calc. 854.91), t R = 8.76 min (HPLC System D). Example 144: 3-Aminobenzvloxvcarbonvl-Tvr(Pθ3H2.-He-Asn-NH-f2-(1 -bromo-naphthalen- 2-yloxy)-ethyl] (SEQ ID NO: 144) Title compound: Mass spectral analysis (negative-ion mode): 884.5 [M-H] + , ( C 39 H 46 N 6°11 P ' calc - 885.71), t R = 8.81 min (HPLC System D). Exaιnple l45: 3-Aminobenzyloxycarbonyl-Tyr(Pθ3H2)-lle-Asn-NH-(3-methyl-butyl) (SEQ ID NO: 145) Title compound: Mass spectral analysis (negative-ion mode): 705.0 [M-H] + , ( c 32 H 47 N 6 o 10 p - calc - 706.74), t R = 7.27 min (HPLC System D). Example 146 3-Aminobenzvloxycarbonyl-Tvr(Pθ3H2.-He-Asn-NH-cyclohexyl (SEQ ID NO: 146) Title compound: Mass spectral analysis (negative-ion mode): 718.4 [M-H] + , ( C 33 H 47 N 6°10 P ' calc - 718.75), t R = 7.23 min (HPLC System D). Example 147: 3-Aminobenzvloxvcarbonvl-Tvr(Pθ3H ? )-AcfiC-Asn-NH-(3-naphthalen-1 -yl- propyl) (SEQ ID NO: 147) The title compound is obtained in analogy to Example 121. Example 148: 3-Aminobenzvloxvcarbonvl-Tvr(Pθ3H2l-Acgc-Asn-NH-(3-naphthalen-2-yl- propyl) (SEQ ID NO: 148) The title compound is obtained in analogy to Example 123. Example 149: 3-Aminobenzyloxvcarbonyl-Tyr(Pθ3H2)-Acgc-Asn-NH-[3-(2-hydroxy- naphthaien-1 -yl)-propyl] (SEQ ID NO: 149) The title compound is obtained in analogy to Example 122. Example 150: Gelatine solution: A sterile-filtered aqueous solution, with 20 % cyclodextrins as solubilisers, of one of the compounds of formula I mentioned in the preceding Examples (e.g. Example 1) as active ingredient, is so mixed under aseptic conditions, with heating, with a sterile gelatine solution containing phenol as preservative, that 1.0ml of solution has the following composition: active ingredient 3 mg gelatine 150.0 mg phenol 4.7 mg dist. water with 20 % cyclodextrins as solubilisers 1.0 ml Example 151 : Sterile dry substance for injection: 5 mg of one of the compounds of formula I mentioned in the preceding Examples (e.g. Example 1 ) as active ingredient are dissolved in 1 ml of an aqueous solution with 20 mg of mannitol and 20 % cyclodextrins as solubilisers. The solution is sterile-filtered and introduced under aseptic conditions into a 2 ml ampoule, deep-frozen and lyophilised. Before use, the lyophilisate is dissolved in 1 ml of distilled water or 1 ml of a physiological saline solution. The solution is administered intramuscularly or intravenously. This formulation can also be introduced into a twin-chambered injection ampoule. Example 152: Nasal spray: 500 mg of finely ground (<5.0 μm) powder of one of the compounds of formula I mentioned in the preceding Examples (e.g. Example 1) is suspended as active ingredient in a mixture of 3.5ml of Myglyol 81 -^ and 0.08 g of benzyl alcohol. The suspension is introduced into a container having a metering valve. 5.0 g of Freon 12! are introduced under pressure into the container through the valve. The "Freon" is dissolved in the Myglyol/benzyl alcohol mixture by shaking. The spray container contains approximately 100 single doses which can be administered individually. Example 153: Film-coated tablets The following ingredients are used for the preparation of 10000 tablets each containing 100 mg of active ingredient: active ingredient 1000 g corn starch 680 g colloidal silica 200 g magnesium stearate 20 g stearic acid 50 g sodium carboxymethyl starch 250 g water quantum satis A mixture of one of the compounds of formula I mentioned in the preceding Examples (e.g. Example 1) as active ingredient, 50 g of corn starch and the colloidal silica is processed with a starch paste, made from 250 g of corn starch and 2.2 kg of demineralised water, to form a moist mass. This is forced through a sieve having a mesh size of 3 mm and dried at 45° for 30min in a fluidised bed drier. The dry granules are pressed through a sieve having a mesh size of 1 mm, mixed with a pre-sieved mixture (1 mm sieve) of 330 g of corn starch, the magnesium stearate, the stearic acid and the sodium carboxymethyl starch, and compressed to form slightly biconvex tablets. Example 154: Incubation of phosphotyrosine protein immobilized on a solid phase with a chimeric SH2-GST (GST = glutathione S-transferase) protein in the presence of a test substance Using the test system mentioned above, and using the phosphorylated "tail" EGFR-MBP fusion protein as ligand, the following IC 50 values are obtained: Example IC 50 1 0.1 2 0.3 3 0.065 4 0.57 5 0.185 6 0.021 7 0.011 8 0.96 9 0.337 10 0.97 14 0.177 15 0.139 17 0.5 21 0.089 22 0.115 24 0.008 26 0.8 34 1 40 0.18 41 0.39 42 0.53 46 0.84 47 0.15 50 0.78 51 0.023 52 0.046 53 0.127 54 0.325 55 0.148 56 0.1 57 0.105 58 0.027 61 0.002 62 0.0026 64 0.035 66 0.33 67 0.034 68 0.68 69 0.54 70 0.35 71 0.13 72 0.007 73 0.076 74 0.018 75 1.96 76 0.1 77 0.14 80 0.014 81 0.009 82 0.99 83 1.9 84 1.0 85 5.9 86 55 87 27.5 89 8.3 90 18.8 91 1.2 92 0.55 93 0.47 94 2.8 95 1.5 96 1.1 97 22.5 98 5.5 99 48.5 100 7.5 101 18.7 102 12.6 103 0.47 104 3.3 106 4.2 107 0.022 108 1.65 111 0.041 112 1.59 113 0.49 114 28.7 115 1.1 116 2.8 117 0.004 118 1.84 119 0.060 120 0.20 121 3.0 122 0.001 123 0.92 124 0.29 125 0.29 126 0.97 128 3.03 129 2.27 130 1.44 131 3.68 132 2.3 133 5.4 134 3.2 135 3.08 136 1.6 138 3.65 142 0.2 143 0.018 145 0.72 147 0.21 148 0.16 SEQUENCE LISTING (1) GENERAL INFORMATION: (i) APPLICANT: (A) NAME: CIBA-GEIGY AG (B) STREET: Klybeckstr. 141 (C) CITY: Basel (E) COUNTRY: Switzerland (F) POSTAL CODE (ZIP): 4002 (G) TELEPHONE: +41 61 69 11 11 (H) TELEFAX: + 41 61 696 79 76 (I) TELEX: 962 991 (ii) TITLE OF INVENTION: Acylated Oligopeptide Derivatives (iii) NUMBER OF SEQUENCES: 151 (iv) COMPUTER READABLE FORM: (A) MEDIUM TYPE: Floppy disk (B) COMPUTER: IBM PC compatible (C) OPERATING SYSTEM: PC-DOS/MS-DOS (D) SOFTWARE: Patentin Release #1.0, Version #1.30 (EPO) (2) INFORMATION FOR SEQ ID NO: 1: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[ (3-aminobenzyloxycarbonyl)-(0-P-Tyr) ]" /note= "O-P-Tyr stands for 0-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 1: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 2: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii) MOLECULE TYPE : peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[ (2-aminobenzyloxyc--rbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-P osphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION : /product== "Gln-NH2 ' (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 2 : Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 3: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATIO :/product= "N-[(3-aminobenzyloxycarbony1)-(O-P-Tyr)]" /note= "O-P-Tyr stands for 0-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 3: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 4: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[(1-(3-aminophenyl)ethoxy-CO)-(O-P-Tyr)]" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 4: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 5: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii ) MOLECULE TYPE : peptide ( ix) FEATURE : (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[ (1-(3-aminophenyl)ethoxy-CO)-(O-P-Tyr) ]" /note= "O-P-Tyr stands for 0-Phosphono-Tyr; diastereomer to SEQ ID:4" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 5: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 6: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii) MOLECULE. TYPE : peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:! (D) OTHER INFORMATION:/product= "N-[ (3-aminobenzyloxycarbonyl)-(O-P-Tyr) ]" /note= "O-P-Tyr stands for 0-Phosphono-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "1-aminocyclopentane-carbonyl" /note= "Radical of 1-Aminocyclopentane carboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 6: Xaa Xaa Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 7: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[(3-aminobenzyl)oxycarbonyl-]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "1-aminocyclohexylcarbonyl" /note= "Radical of 1-amincyclohexane carboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 7: Xaa Xaa Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 8: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATIO :/product= "N-[2-(4-methyl-5-thiazolyl)ethoxy-CO]-PTyr' /note= "PTyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 8: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 9: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[2-(3-hydroxyphenyl)ethoxyccirbonyl]-PTyr" /note= "PTyr stands for 0-Phospono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 9: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 10: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[3-hydroxybenzyloxycirbonyl]-O-P-Tyr" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS I (D) OTHER INFORMATIO :/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 10: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 11: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[3-aminobenzyloxycarbonyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "1-aminocyclohexylcarbonyl" /note= "Bivalent radical of 1-aminocyclohexane carboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "bAla-NH2" /note= "bAla stands for beta-Alanyl (-NH-CH2-CH2-(C=0)-)" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 11: Xaa Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 12: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[3-aιr nobenzyloxycarbonyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "1-aminocyclohexylcarbonyl" /note= "Bivalent radical of 1-aminoσyclohexyl carboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gly-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 12: Xaa Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 13: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATIO :/product= "N-[benzyloxycarbonyl]-(O-P-Tyr) " /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 13: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 14: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide ( ix ) FEATURE : (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[3,5-diaminobenzyloxycarbonyl]-(PTyr)" /note= "PTyr stεinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 14: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 15: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[3-(3-indolyl)-propionyl]-(O-P-Tyr) " /note= "O-P-Tyr stands for O-Phosphono-L-Tyr' (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATIO :/product= "Gln-NH2' (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 15: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 16: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[3-(N-acetylamino)phenoxyacetyl]-PTyr" /note= "PTyt stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 16: Xaa Ile Asn Xaa (2) INFORMATION FOR SEQ ID NO: 17: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATIO :/product= "N-[4-( -acetylamino)phenoxyacetyl]-PTyr" /note= "PTyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 17: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 18: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATIO :/product= "N-[(2-acetylamino)-phenoxyacetyl]-PTyr" /note= "PTyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 18: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 19: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATIO :/product= "N-[4-aminophenoxyacetyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 19: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 20: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Active-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[3-aminophenoxyacetyl]-(O-P-Ty )" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 20: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 21: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-(3-indolyl)butyroyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 21: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 22: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[(3-indolyl)-acetyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 22: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 23: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii ) MOLECULE TYPE : peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[benzoyi]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 23: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 24: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" ( ix ) FEATURE : (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 24: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 25: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: -imino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[benzimidazol-5-ylcarbonyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 25: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 26: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[2-amino-thiazol-4-yl-acetyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr' (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 26: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 27: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-cyanobenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATIO :/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 27: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 28: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 ainino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii) MOLECULE TYPE : peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION : 1 (D) OTHER INFORMATION: /product= "N- [ 2 , 3-dihydrobenzofuran-5-yl-CO] -PTyr " /note= "PTyr stands for P-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 28: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 29: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-hydroxybenzoyl]-(O-P-Tyr) " /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION : /product= "Gln-NH2 " (xi ) SEQUENCE DESCRIPTION: SEQ ID NO: 29 : Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 30: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-methoxybenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 30: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 31: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-methylthio-benzoyl]-(O-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 31: Xaa Ile Asn Xaa (2) INFORMATION FOR SEQ ID NO: 32: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-methylsulfinyl-benzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 32: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 33: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[imidazol-4-yl-acryloyl]-(O-P-Tyr)' /note= "O-P-Tyr stands for O-Phosphono-L-Tyr ; trains isomer" ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATIO :/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 33: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 34: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-(N-methylamino)-benzoyi]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 34: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 35: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-(N,N-dirrethylaminobenzoyl) ]-(0-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 35: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 36: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[pyridin-4-carbonyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 36: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 37: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminomethylbenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 37: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 38: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-amino-3-methoxybenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr", (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 38: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 39: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminophenylacetyl] -(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 39: Xaa Ile Asn Xaa (2) INFORMATION FOR SEQ ID NO: 40: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[3-aminobenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 40: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 41: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[quinoline-6-yl-carbonyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 41: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 42: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:! (D) OTHER INFORMATION:/product= "N-[4-methoxycarbonyl-benzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 42: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 43: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-carboxy-benzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 43: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 44: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-amino-2-chlorobenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyt" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 44: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 45: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[6-aminonicotinoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 45: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 46: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-amino-3-hydroxybenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 46: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 47: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[3-(3-aminophenyl)propionyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 47: Xaa Ile Asn Xaa (2) INFORMATION FOR SEQ ID NO: 48: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION: /product= " N- [ 4-eiminobenzoyl ] - ( O-P-Tyr ) " /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Ile-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 48: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 49: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION: /product= "N- [ indole-3-yl-acryloyl ] - ( O-P-Tyr ) " /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr; trans-isomer" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 49: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 50: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(O-P-Tyr) " /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 50: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 51: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(O-P-Tyr) " /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 51: Xaa Asp Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 52: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(O-P-Tyr) " /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION: 4 (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 52: Xaa Gly Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 53: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for C—Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gly-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 53: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 54: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Val-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 54: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 55: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asp-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 55: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 56: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:! (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(O-P-Tyr)' /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "1-aminocyclopentane-carbamide" /note= "Radical of 1-aminocyclopentane carboxylic acid with carboxy-group (CCOH) in carbamide (CONH2) form" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 56: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 57: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 57: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 58: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "bAla-NH2" /note= "radical of beta-alanyl-amide (-NH-CH2-CH2-(C=0)-)" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 58: Xaa Ile Asn Xaa (2) INFORMATION FOR SEQ ID NO: 59: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION: /product= "N- [ 4--ιminobenzoyl ] - ( O-P-Tyr ) " /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 59: Xaa Ile Gly Xaa 1 (2) INFORMATION FOR SEQ ID NO: 60: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 60: Xaa Ile Gin Xaa 1 (2) INFORMATION FOR SEQ ID NO: 61: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:! (D) OTHER INFORMATION:/product= "N-[indole-5-yl-carbonyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 61: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 62: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATIO :/product= "N-[indole-5-yl-carbonyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 62: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 63: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[indole-5-ylσarbonyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "1-aminocyclohexane-carbonyl" /note= "Radical of 1-aminocyclohexane carboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 63: Xaa Xaa Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 64: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[3-aminobenzyloxycarbonyl]-(L-CF2Pmp)" /note= "L-CF2-Pmp steinds for 4-Phosphonodifluoromethyl-L-Phe' (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 64: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 65: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(L-F2Pmp)" /note= "L-F2Pmp stands for 4-(phosphono-difluoromethyl)-L-Phe" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 65: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 66: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE : (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-[4-aminobenzoyl]-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modif ied-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 66: Xaa Phe Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 67: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" ( ix ) FEATURE : (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 67: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 68: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "[N-(trans-3-hydroxy-cinnamoyl)-(O-P-Tyr)]" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 68: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 69: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "[N-(t-3-h-4-m-cinnamoyl)-(O-P-Tyr)]" /note= "t-3-h-4-h-m-cinnamoyl stands for trans-3-hydroxy-4-methoxy-cinnamoyl); O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 69: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 70: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)' (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATIO :/product= "Ile-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 70: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 71: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "1-aminocyclohexane-carbonyl" /note= "Radical of 1-aminocyclohexane carboxylic acid" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 71: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 72: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "1-aminocyclohexane-carbonyl" /note= "Radical of 1-aminocyclohexane cεirboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 72: Xaa Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 73: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-7,8-di-OH-2-0-2H-benzopyran-CO-(O-P-Tyr)" /note= "7,8-di-OH-2-0-2H-benzopyran-CO stands for 7,8-dihydroxy-2-oxo-2H-(benzopyra )-3-carboxyl; O-P-Tyr steinds for O-Phosphono-L-Tyr" ( ix) FEATURE : (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2' (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 73: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 74: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-tr-ms-3,4-dihydroxy-cir-namoyl-(O-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 74: Xaa Met Xaa 1 (2) INFORMATION FOR SEQ ID NO: 75: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 75: Xaa Pro Xaa 1 (2) INFORMATION FOR SEQ ID NO: 76: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "3-(3,4-dihydroxyphenyl) ropionyl-(O-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 76: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 77: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-2-(3,4-dihydroxyphenyl)acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 77: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 78: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B ) LOCATIONS (D) OTHER INFORMATION : /product= "Gly-Nh2 ' (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 78 : Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 79: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxycinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "beta-alanyl" /note= "beta-alanyl stands for -NH-CH2-CH2-C(=0)-" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 79: Xaa Xaa (2) INFORMATION FOR SEQ ID NO: 80: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinn-ιmoyl-(O-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "1-amino-cycloheptane-carbonyl" /note= "Radical of 1-Aminocycloheptane carboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 80: Xaa Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 81: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:! (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "-2-amino-2-nornornane-carbonyl-" /note= "Radical of 2-amino-2-norbornane carbonic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 81: Xaa Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 82: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-σinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "-2-aιr-ino-2-norbornane-carbonyl-" /note= "Radical of 2-amino-2-norbornane carboxylic acid; epimer 1" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 82: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 83: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "-2-amino-2-norbornane-carbonyl" /note= "Bivalent radical of 2-amino-2-norbornane carboxylic acid (epimer 2)" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 83: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 84: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-4-hydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 84: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 85: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-6-hydroxy-2-naphthoyl-(O-P-Tyr)' /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Ile-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 85: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 86: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 86: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 87: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Glu-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 87: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 88: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "D-homophenylalanyl" /note= "Radical of D-Homophenylalanine" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 88: Xaa Glu Xaa 1 (2) INFORMATION FOR SEQ ID NO: 89: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide ( ix) FEATURE : (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "D-homophenylalanyl-NH2' /note= "Radical of D-homophenylalanine-amide" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 89: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 90: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATIO :/product= "1-aminocyclopentane-carbonyl" /note= "Radical of 1-aminocyclopentane carboxylic acid" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 90: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 91: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Pro-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 91: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 92: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: -imino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-2-naphthoyl-(O-P-Tyr)' /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 92: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 93: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(1-adamantoyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 93: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 94: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide ( ix ) FEATURE : (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-cyclohexanoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 94: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 95: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(3-cyclohexyl-propionyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Ile-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 95: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 96: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-l,2,3,4-tetrahydro-2-naphthoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Ile-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 96: Xaa Xaa (2) INFORMATION FOR SEQ ID NO: 97: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-cyclohexanoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Ile-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 97: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 98: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(2-naphthoyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Ile-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 98: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 99: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:! (D) OTHER INFORMATION:/product= "N-(1-adamantoyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Ile-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 99: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 100: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATIO :/product= "N-(4-acetylamino-benzoyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Ile-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 100: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 101: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(succinamoyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 101: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 102: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-l,2 ,3,4-tetrahydro-2-naphthoyl-(O-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 102: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 103: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii ) MOLECULE TYPE : peptide ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-l,2,3,4-tetrahydro-2-naphthoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Pro-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 103: Xaa Ile Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 104: (i) SEQUENCE CHARACTERISTICS: (A) I-ENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "-homophenylalanyl-NH2" /note= "Radical of the amide of L-homophenylalanine" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 104: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 105: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 105: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 106: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phospho-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "beta-alanyl-NH2" /note= "Beta-alanyl-NH2 stands for -NH-CH2-CH2-C(=0)-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 106: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 107: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gln-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 107: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 108: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-trans-3,4-dihydroxy-cinnamoyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Gly-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 108: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 109: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION : /product= "N-trans-3 , 4-dihydroxyciιιnamoyl- ( L-CF2-Pm ) " /note= "L-CF2-Pmp steinds for 4-Phosphonodifluormethyl-L- Phe" ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 109: Xaa Ile Xaa (2) INFORMATION FOR SEQ ID NO: 110: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATIO :/product= "N-trans-3,4-dihydroxy-cinnamoyl-(L-CF2Pmp)" /note= "L-CF2Pmp stands for 4-Phosphonodifluormethyl-L- Phe" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) -LOCATION: 2 (D) OTHER INFORMATION:/product= "Ile-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 110: Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 111: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(3-aminobenzyloxycarbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 111: Xaa Met Xaa 1 (2) INFORMATION FOR SEQ ID NO: 112: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(indole-5-carbonyl)-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 112: Xaa Ile Asn Xaa 1 (2) INFORMATION FOR SEQ ID NO: 113: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-cyclohexylcarbonyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATIO :/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 113: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 114: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(2-naphthylcarbonyl)-(O-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 114: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 115: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(indole-5-yl-carbonyl)-(L-CF2Pmp)" /note= "L-CF2Pmp stands for 4-Phosphonodifluormethyl-L- Phe" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 115: Xaa Ile Xaa (2) INFORMATION FOR SEQ ID NO: 116: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(9-fluorenyl-carbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr' (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 116: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 117: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(3-aminobenzyloxycarbonyl)-(O-P-Tyr) " /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 117: Xaa Gin Xaa 1 (2) INFORMATION FOR SEQ ID NO: 118: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:! (D) OTHER INFORMATION: /product= " N- ( 3-ciminobenzyloxycarbonyl ) - ( O-P-Tyr ) " /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATIO :/product= "L-alpha-tert-butyl-Gly" /note= "Radical of L-alpha-tert-butyl-glycine" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 118: Xaa Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 119: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(3-amino-benzyloxycarbonyl)-(Pmp)" /note= "Pmp stands for the radical -(4-Phosphonomethyl- Phe)-" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 119: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 120: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(3-aminobenzyloxycarbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyrosine" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "1-aminocyclohexane-carbonyl" /note= "Radical of 1-aminocyclohexane carboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH2" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 120: Xaa Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 121: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(3-naphthalen-l-yIpropyl) " /note= "alfa-(3-Naphthalen-l-yl-propyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 121: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 122: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(3-(2-hydroxynaphthalen-l-yl)propyl" /note= "radical of alfa-(N-(3-(2-hydroxynaphthalenl-yl)propylamide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 122: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 123: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-HN-(3-naphthalen-2-yl-propyl)" /note= "Radical of alfa-N-(3-naphthalen-l-yl-propyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 123: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 124: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-HN-(3-phenanthren-9-yl-propyl)" /note= "Radical of alfa-N-(3-phenanthren-9-yl-propyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 124: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 125: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 -imino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide ( ix) FEATURE : (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-1-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATIO :/product= "Asn-HN-(2-(l-bromonaphthalen-2-yloxy)ethyl" /note= "Radical of alfa-N-(2-(l-bromonaphthalen-2- yloxy)ethyl amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 125: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 126: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= " -acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(3,3-dipheny1-propyl)" /note= "Radical of alfa-N-(3,3-diphenyl)propyl amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 126: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 127: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-3-phenyIpropyl" /note= "Radical of alfa-N- ( 3-pheny Ipropyl) amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 127 : Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 128: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: -imino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-HN-(3-(2,4-dichlorophenyl)propyl" /note= "Radical of alfa-N-(3-(2,4-dichlorophenyl- propyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 128: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 129: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii) MOLECULE TYPE : peptide ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(2,2-diphenyl-ethyl)" /note= "Radical of alfa-N-(2,2-diphenyl-ethyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 129: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 130: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATIO :/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(2-(4-chlorophenyl)ethyl)" /note= "Radical of alfa-N-(2-(4-chlorophenyl)ethyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 130: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 131: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide ( ix) FEATURE : (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr) " /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-benzyl" /note= "Radical of alfa-N-benzylamide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 131: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 132: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide [ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-isobutyl" /note= "Radical of Alfa-N-isobutylamide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 132: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 133: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(3-methylbutyl)" /note= "Radical of alfa-N-(3-methylbutyl)-imide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 133: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 134: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(2-ethyl-hexyl)" /note= "Radical of alfa-N-(2-ethyl-hexyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 134: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 135: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(cyclohexyl)" /note= "Radical of alfa-N-(cyclohexyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 135: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 136: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(cyclohexylmethyl)" /note= "Radical of alfa-N-cyclohexylamide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 136: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 137: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION :/product= " 1-aminocyclohexane-carbonyl " /note= "Radical of 1-Aminocyclohexane carboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= " sn-NH-(3-naphthalen-l-yl-propyl)" /note= "Radical of alfa-N-(3-naphthalen-l-yl-propyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 137: Xaa Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 138: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 -imino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" ( ix) FEATURE : (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "1-amino-cyclohexylcarbonyl" /note= "Radical of 1-amino-cyclohexane carboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(3-naphthalen-2-yl-propyl)" /note= "Radical of alfa-N-(3-naphthalen-2-yl-propyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 138: Xaa Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 139: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-acetyl-(O-P-Tyr) " /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/products "1-a-ι-ino-cyclohexylcarbonyl" /note= "Radical of 1-amino-cyclohexane carboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(3-(2-hydroxynaphthalen-lyi)propyl)" /note= "Radical of alfa-N-(3-(2-hydroxynaphthalen-1-yl)propyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 139: Xaa Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 140: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:! (D) OTHER INFORMATION:/product= "N-(3-aminobenzyloxycarbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION : /product= "Asn-NH- ( 3-naphthalen-l-yl-propyl ) " /note= "Radical od alfa-N- ( 3-naphthalen-l-yl-propyl) amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 140: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 141: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(3-aminobenzyloxycarbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:3 (D) OTHER INFORMATION:/product= "Asn-NH-(3-(2-hydroxynaphthalen-lyl)propyl)" /note= "Radical of alfa-N-(3-(2-hydroxy-naphthalen-l-yl)propyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 141: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 142: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(3-aminobenzyloxycarbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION : /product= " Asn-N- ( 3-naphthalen-2 -yl-propyl ) " /note= "Radical of alfa-N-(3-naphthalen-2-yl-propyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 142: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 143: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: -imino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:l (D) OTHER INFORMATION:/product= "N-(3-aminobenzyloxycarbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(3-phenanthren-9-yl-propyl)" /note= "Radical ofalfa-N-(3-phenanthren-9-yl-propyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 143: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 144: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-2-(l-bromonaphthalen-2-yl-oxy)ethyl" /note= "Radical of alfa-N-(2-(2-bromonaphthalen-2-yl-ox )ethyl)amide of Asn" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(3-aminobenzyloxycarbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 144: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 145: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(3-aminobenzyloxycarbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(3-methyl-butyl)" /note= "Radical of alfa-N-(3-methyl-butyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 145: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 146: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(3-aminobenzyloxycarbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER nϊFORMATION:/product= "Asn-NH-cyclohexyl" /note= "Radical of alfa-N-(cyclohexyl)-imide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 146: Xaa Ile Xaa 1 (2) INFORMATION FOR SEQ ID NO: 147: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N- ( 3-aminobenzy loxycarbonyl ) - ( O-P-Tyr ) " /note= "O-P-Tyr steinds for O-Phosphono-L-Tyr" ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "-1-amino-cyclohexylcarbonyl-" /note= "Radical of 2-aminocyclohexane carboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION: /product= "Asn-NH- ( 3-naphthalen-l-yl-carbonyl ) " /note= "Radical of alfa-N- ( 3-nephthalen-l-ylcarbonyl) amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 147: Xaa Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 148: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(3-aminobenmzyloxycarbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION: /product= " - 1-aιnino-cyclohexalcarbonyl- " /note= "Radical of 1-amino-cyclohexane carboxylica acid" ( ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(3-naphthalen-2-ylpropyl)" /note= "Radical of alfa-N-(3-naphthalen-2-yl-propyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 148: Xaa Xaa Xaa 1 (2) INFORMATION FOR SEQ ID NO: 149: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 3 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATION:1 (D) OTHER INFORMATION:/product= "N-(3-aminobenzyloxycarbonyl)-(O-P-Tyr)" /note= "O-P-Tyr stands for O-Phosphono-L-Tyr" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATIO :/product= "-1-amino-cyclohexylcarbony1-" /note= "Radical of 1-aminocyclohexane carboxylic acid" (ix) FEATURE: (A) NAME/KEY: Modified-site (B) LOCATIONS (D) OTHER INFORMATION:/product= "Asn-NH-(3-(2-hydroxynaphthalen-lyl)propyl)" /note= "Radical of alfa-N-(3-(2-hydroxy-naphthalen-l-yl)propyl)amide of Asn" (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 149: Xaa Xaa Xaa 1

Claims: What is claimed is 1. A compound of the formula I, X- ■ <AA) n . • PTI ' (I) wherein n is 0 to 15, X is arylcarbonyl, cycloalkylcarbonyl, tricycloalkylcarbonyl, arylsulfonyl, heterocyclylcarbonyl, heterocyclylsulfonyl, carbamoyl-lower alkanoyl, aryl-lower alkylcarbonyl, cycloalkyl-lower alkylcarbonyl, aryl-lower alkylsulfonyl, heterocyclyl-lower alkylcarbonyl, heterocyclyl-lower alkylsulfonyl with the proviso that in any of the lower alkyl radicals mentioned a methylene group may be replaced with oxa, aza or thia; heterocyclyl-lower alkenylcarbonyl or aryl- lower-alkenylcarbonyl; or, if Y is a secondary or tertiary amino group, is one of the morieties X mentioned above or lower alkanoyl, halo-lower alkanoyl, lower-alkoxycarbonyl, aryl-lower alkoxycarbonyl or cycloalkyl-lower alkoxycarbonyl; PTI is the bivalent radical of tyrosine or (preferably) the bivalent radical of phosphotyrosine or a phosphotyrosine mimic, AA stands for a bivalent radical of a natural or unnatural amino acid, and Y is hydroxy, a C-terminal protecting group or a primary, secondary or tertiary amino group, or a salt thereof. 2. A compound of formula I according to claim 1 , wherein n is 1 to 15, 237 X is arylcarbonyl, cycloalkylcarbonyl, arylsulfonyl, heterocyclylcarbonyl, heterocyclylsulfonyl; aryl-lower alkylcarbonyl, cycloalkyl-lower alkylcarbonyl, aryl-lower alkylsulfonyl, heterocyclyl- lower alkylcarbonyl, heterocyclyl-lower alkylsulfonyl with the proviso that in any of the lower alkyl radicals mentioned a methylene group may be replaced with oxa, aza or thia; or heterocyclyl-lower alkenylcarbonyl, PTI is the bivalent radical of phosphotyrosine or a phosphotyrosine mimic, AA stands for a bivalent radical of a natural or unnatural amino acid, and Y is hydroxy, a C-terminal protecting group or a primary, secondary or tertiary amino group, or a salt thereof. 3. A compound of formula I according to claim 1 wherein n is 1 to 4; X is selected from (i) benzoyi or benzoyi substituted with amino; lower alkylamino; amino-lower alkyl; hydroxy; lower alkoxy; amino and hydroxy; amino and lower alkoxy; carboxy; lower- alkoxycarbonyl; cyano; halogen; lower-alkylthio; or lower alkylsulfinyl; (ii) naphthoyl, hydroxy-naphthoyi or fluorenylcarbonyl; (iii) cyclohexylcarbonyl or 1 ,2,3,4-tetrahydronaphthyl-2-carbonyl; (iv) tricyclo[5.2.1.0 2,6 ]dec-8-ylcarbonyl or adamantoyl; ...(v) pyridylcarbonyl which is unsubstituted or substituted with amino, benzimidazolyl¬ carbonyl, quinolinyl-carbonyl, 2,3-dihydrobenzofuranylcarbonyl, and indolylcarbonyl; (vi) chromenylcarbonyl that is unsubstituted by 1 to 3 substitutents selected from oxo and hydroxy; (vii) carbamoyl-lower alkanoyl; (vii) phenyl-methoxycarbonyl wherein the phenyl residue is unsubstituted or substituted with amino in the 2-, 3- and 5-, 4- or 3-position of the phenyl ring; (±)-, (+) or (-)-1-(3- aminophenyl)ethyloxycarbonyl; hydroxybenzyloxy- or hydroxyphenyl-2-ethoxycarbonyl; - 238 lower alkanoylamino-phenyloxymethylcarbonyl; aminophenyloxymethylcarbonyl; aminophenyl-lower alkylcarbonyl; benzyl-oxycarbonyl or phenylacetyl; (viii) dihydroxyphenyl-lower alkylcarbonyl; (ix) cyclohexyl-lower alkylcarbonyl; (x) unsubstituted or lower alkyl-substituted 2-(thiazolyl)-ethoxycarbonyl, unsubstituted or amino-substituted thiazolyl-lower alkylcarbonyl or indolyl-lower alkylcarbonyl; (xi) imidazolyl-lower alkenylcarbonyl, or indolyl-lower alkenylcarbonyl; (xii) cinnamoyi substituted by 1 to 2 moieties selected independently from methoxy and especially hydroxy; and (xiii) if Y is secondary or tertiary amino, also from lower alkanoyl; PTI is a bivalent radical of tyrosine or (preferably) a bivalent radical of phosphotyrosine or of a phosphotyrosine mimic in the form of a bivalent radical of an amino acid selected from phosphonomethyl-phenylalanine, phosphono-(α-fluoro)methyl-phenylalanine, phosphono- (α,α-difluoro)methyl-phenylalanine, phosphono-(α-hydroxy)methyl-phenylalanine, O-sulfo- tyrosine, dicarboxymethoxy-phenylalanine, aspartic acid, glutamic acid, phosphoserine and phosphothreonine, each of which is present in the (D,L)-, D- or preferably the L-form; -(AA) n - has one of the following meanings: • A bivalent radical of a tripeptide of the formula -(AA 1 )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is selected from -He-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly-, -Phe-, -Ac^-, -Nbo-, -Met-, -Pro-, -βAla-, - Gin-, -Glu-, -DHph-, -HPh- and -tie-; -(AA 2 )- is selected from -Asn-, -βAla-, -Gly-, -lie-, -βAla- and Gin; and -(AA 3 )- is selected from -Val-, -β-Ala, -Gly-, -Gin-, -Val-, -Asp- and - Ac 5 c- ; or, • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- and -(AA 2 )- preferably have the meanings given above; and -(AA 2 )- being -Asn- or -βAla-; • or simply a bivalent radical of an amino acid selected from the amino acids mentioned above;. and Y is amino (-NH 2 ) or monosubstituted amino selected from lower alkylamino; octylamino; halonaphthyloxy-lower alkylamino, naphthyloxy-lower alkylamino; phenyl-lower alkylamino, di-phenyl-lower alkylamino; (mono- or di-halo-phenyl)-lower alkylamino; naphthalenyl-lower alkylamino; hydroxy-naphthalenyl-lower alkylamino, phenanthrenyl-lower alkylamino; cycloalkylamino; and cycloalkyl-lower alkylamino; or a salt thereof where at least one salt-forming group is present. 4. A compound of formula I according to claim 1 wherein n is 1 to 4; X is selected from (i) benzoyi or from benzoyi substituted with amino; lower alkylamino; amino-lower alkyl; hydroxy; lower alkoxy; amino and hydroxy; amino and lower alkoxy; carboxy; lower- alkoxycarbonyl; cyano; halogen, lower-alkylthio; or lower alkylsulfinyl; (ii) pyridylcarbonyl which is unsubstituted or substituted with amino, benzimidazolylcarbonyl, quinolinyl-carbonyl, 2,3-dihydrobenzofuranylcarbonyl, or indolylcarbonyl; (iii) phenyl-methoxycarbonyl wherein the phenyl residue is unsubstituted or substituted with amino in the 2-, 3- and 5-, 4- or 3-position of the phenyl ring; (±)-, (+) or (-)-1-(3- aminophenyl)ethyloxycarbonyl; hydroxybenzyloxy- or hydroxyphenyl-2-ethoxycarbonyl, lower alkanoylamino-phenyloxymethylcarbonyl, aminophenyloxymethylcarbonyl, aminophenyl-lower alkylcarbonyl, benzyl-oxycarbonyl or phenylacetyl; (iv) unsubstituted or lower alkyl-substituted 2-(thiazolyl)-ethoxycarbonyl, unsubstituted or amino-substituted thiazolyl-lower alkylcarbonyl or indolyl-lower alkylcarbonyl, and (v) imidazolyl-lower alkenylcarbonyl or indolyl-lower alkenylcarbonyl; PTI is a bivalent radical of phosphotyrosine or of a phosphotyrosine mimic in the form of a bivalent radical (which is bound N-terminally via the imino group resulting from the α-amino group and C-terminally via the carbonyl group resulting from its α-carboxy group) of an amino acid selected from phosphonomethyl-phenylalanine, phosphono-(α-fluoro)methyi- phenylalanine, phosphono-(α,α-difluoro)methyl-phenylalanine, phosphono-(α-hydroxy)- methyl-phenylalanine, O-sulfo-tyrosine, dicarboxymethoxy-phenylalanine, aspartic acid, glutamic acid, phosphoserine and phosphothreonine, each of which is present in the (D,L)-, D- or preferably the L-form; -(AA) n - has one of the following meanings: • a bivalent radical of a tripeptide of the formula -(AA 1 )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is selected from -He-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly- and -Phe-, -(AA 2 )- is selected from -Asn-, and also from -βAla- and -Gly-, most preferably -Asn-; and -(AA 3 )- is selected from -Val-, -β-Ala-, -Gly-, -Gin-, -Val-, -Asp- and -Ac 5 c- ; • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- is -lie- or -Ac 6 c- and -(AA 2 )- is -Asn- or -βAla-; • or simply a bivalent radical of the amino acid selected from the amino acids mentioned above, especially -He-; and Y is a free amino group, a mono- or disubstituted amino group the substituents of which are selected from the group comprising lower alkyl, phenyl-lower alkyl, pyrrolidinyl-lower alkyl, pyridyl-lower alkyl, furyl-lower alkyl, morpholinyl-lower alkyl and indolyl-lower alkyl, or is 1- pyrrolidinyl or 4-morpholinyl, or a salt thereof. 5. A compound of formula I according to claim 1 wherein n is 1 to 4; X is selected from (i) naphthoyl, hydroxy-naphthoyi or fluorenylcarbonyl; (ii) cyclohexylcarbonyl or 1 ,2,3,4-tetrahydronaphthyl-2-carbonyl; (iii) tricyclo[5.2.1.0 2,6 ]dec-8-ylcarbonyl or adamantoyl; (iv) chromenylcarbonyl that is unsubstituted by 1 to 3 substitutents selected from oxo and hydroxy; (v) carbamoyl-lower alkanoyl; (vi) dihydroxyphenyl-lower alkylcarbonyl; (vii) cyclohexyl-lower alkylcarbonyl; and (viii) cinnamoyi substituted by 1 to 2 moieties selected independently from methoxy and hydroxy; and (ix) if Y is secondary or tertiary amino, also from lower alkanoyl; - 241 - PTI is a bivalent radical of tyrosine or a bivalent radical of phosphotyrosine or of a phosphotyrosine mimic in the form of a bivalent radical of an amino acid selected from phosphonomethyl-phenylalanine, phosphono-(α-fluoro)methyl-phenylalanine, phosphono- (α,α-difluoro)methyl-phenylalanine, phosphono-(α-hydroxy)methyl-phenylalanine, O-sulfo- tyrosine, dicarboxymethoxy-phenylalanine, aspartic acid, glutamic acid, phosphoserine and phosphothreonine, each of which is present in the (D,L)-, D- or the L-form; -(AA) n - has one of the following meanings: • A bivalent radical of a tripeptide of the formula -(AA 1 )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is selected from -He-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly-, -Phe-, -Ac^-, -Nbo-, -Met-, -Pro-, -βAla-, - Gin-, -Glu-, -DHph-, -HPh- and -tLe-; -(AA 2 )- is selected from -Asn-, -βAla-, -Gly-, -He-, -βAla- and Gin; and -(AA 3 )- is selected from -Val-, -β-Ala, -Gly-, -Gin-, -Val-, -Asp- and - Ac 5 c- ; or • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- and -(AA 2 )- preferably have the meanings given above,; and -(AA 2 )- being -Asn- or -βAla-; • or simply a bivalent radical of an amino acid selected from the amino acids mentioned above; and Y is amino (-NH 2 ) or monosubstituted amino selected from lower alkylamino; octylamino; halonaphthyloxy-lower alkylamino, naphthyloxy-lower alkylamino; phenyl-lower alkylamino, di-phenyl-lower alkylamino, (mono- or di-halo-phenyl)-lower alkylamino, naphthalenyl-lower alkylamino, hydroxy-naphthalenyl-lower alkylamino or phenanthrenyl-lower alkylamino; cycloalkylamino; and cycloalkyl-lower alkylamino; or a salt thereof where at least one salt-forming group is present. 6. A compound of formula I according to claim 1 wherein n is 1 , 2 or 3; X is selected from 4-aminobenzoyl, 3-aminobenzoyl, 4-amino-2-hydroxy-benzoyl, 4-lower alkoxycarbonyl-benzoyl, quinolinyl-carbonyl, indolylcarbonyl; phenyl-methoxycarbonyl wherein the phenyl residue is unsubstituted or substituted with amino in the 2-, 3- and 5-, 4 or 3-position of the phenyl ring; (+)-, (+) or (-)-1-(3-aminophenyl)ethyloxycarbonyl; hydroxy- benzyloxy- or hydroxyphenyl-2-ethoxycarbonyl; unsubstituted or lower alkyl-substituted 2- (thiazolyl)-ethoxycarbonyl, unsubstituted or amino-substituted thiazolyl-lower alkylcarbonyl, indolyl-lower alkylcarbonyl, naphthoyl or hydroxy-naphthoyi, cyclohexylcarbonyl, 1,2,3,4- tetrahydronaphthyl-2-carbonyl, adamantoyl, 7,8-dihydroxy-2-oxo-2H-(benzopyran)-3-yl- carbonyl, carbamoyl-lower alkanoyl, dihydroxyphenyl-lower alkylcarbonyl and cinnamoyi substituted by 1 to 2 moieties selected independently from methoxy and hydroxy; and, if Y is monosubstituted amino, also from lower alkanoyl; PTI is a bivalent radical of phosphotyrosine or of a phosphotyrosine mimic of the phosphono-(α,α-difluoro)methyl-phenylalanine or the phosphonomethyl-phenylalanine type, -(AA) n - has one of the following meanings: • A bivalent radical of a tripeptide of the formula -(AA )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is selected from -He-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly-, -Phe-, -Ac 7 c-, -Nbo-, -Met-, -Pro-, -βAla-, - Gin-, -Glu-, -DHph-, -HPh- and -tLe-; -(AA 2 )- is selected from -Asn-, -βAla-, -Gly-, -He-, -βAla- and Gin; and -(AA 3 )- is selected from -Val-, -β-Ala, -Gly-, -Gin-, -Val-, -Asp- and - Ac 5 c- ; or • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- and -(AA 2 )- preferably have the meanings given above; and -(AA 2 )- being -Asn- or -βAla-; • or simply a bivalent radical of an amino acid selected from the amino acids mentioned above; and Y is amino (-NH 2 ) or monosubstituted amino selected from lower alkylamino; octylamino; halonaphthyloxy-lower alkylamino, or naphthyloxy-lower alkylamino; phenyl-lower alkylamino, (mono- or di-halo-phenyl)-lower alkylamino, naphthalenyl-lower alkylamino, hydroxy-naphthalenyl-lower alkylamino or phenanthrenyl-lower alkylamino; cycloalkylamino; and cycloalkyl-lower alkylamino; or a salt thereof where at least one salt-forming group is present. 7. A compound of formula I according to claim 1 wherein n is 2 or 3; X is selected from 4-aminobenzoyl, 3-aminobenzoyl, 4-amino-2-hydroxy-benzoyl, 4-lower alkoxycarbonyl-benzoyl, quinolinyl-carbonyl, indolylcarbonyl, phenyl-methoxycarbonyl wherein the phenyl residue is unsubstituted or substituted with amino in the 2-, 3- and 5-, 4- or 3-position of the phenyl ring; (±)-, (+) or (-)-1-(3-aminophenyl)ethyloxycarbonyl; hydroxybenzyloxy- or hydroxyphenyi-2-ethoxycarbonyl, unsubstituted or lower alkyl- substituted 2-(thiazolyl)-ethoxycarbonyl, unsubstituted or amino-substituted thiazolyl-lower alkylcarbonyl, and indolyl-lower alkylcarbonyl, PTI is a bivalent radical of phosphotyrosine or of a phosphotyrosine mimic of the phosphono-(α,α-difluoro)methyl-phenylalanine type, -(AA) n - has one of the following meanings: • a bivalent radical of a tripeptide of the formula -(AA 1 )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is selected from -He-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly- and -Phe-, most preferably -He-, -Ac 5 c-, -Ac 6 c-, -Asp- or -Gly-; -(AA 2 )- is selected from -Asn-, and also from -βAla- and -Gly-, most preferably -Asn-; and -(AA 3 )- is selected from -Val-, -β-Ala, -Gly-, -Gin-, -Val-, -Asp- and -Ac 5 c- ; or • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- is-lle- or -Ac 6 c- and -(AA 2 )- is-Asn- or -βAla-; and Y is a free amino group, or a salt thereof. 8. A compound of formula i according to claim 1 wherein n is 1 , 2 or 3; X is selected from naphthoyl or hydroxy-naphthoyi; cyclohexylcarbonyl, 1 ,2,3,4- tetrahydronaphthyl-2-carbonyl, adamantoyl, 7,8-dihydroxy-2-oxo-2H-(benzopyran)-3-yl- carbonyl, carbamoyl-lower alkanoyl, dihydroxyphenyl-lower alkylcarbonyl, and cinnamoyi substituted by 1 to 2 moieties selected independently from methoxy and especially hydroxy; and, if Y is monosubstituted amino, also from lower alkanoyl; PTI is a bivalent radical of phosphotyrosine or of a phosphotyrosine mimic of the phosphono-(α,α-difluoro)methyl-phenylalanine or the phosphonomethyl-phenylalanine type; -(AA) n - has one of the following meanings: • A bivalent radical of a tripeptide of the formula -(AA 1 )-(AA 2 )-(AA 3 )- wherein -(AA 1 )- is selected from -lie-, -Ac 5 c-, -Ac 6 c-, -Asp-, -Gly-, -Phe-, -Ac-rC-, -Nbo-, -Met-, -Pro-, -βAla-, - Gin-, -Glu-, -DHph-, -HPh- and -tLe-; -(AA 2 )- is selected from -Asn-, -βAla-, -Gly-; and -(AA 3 )- is selected from -Val-, -β-Ala, -Gly-, -Gin-, -Val-, -Asp- and -Ac 5 c- ; or • a bivalent radical of a dipeptide of the formula -(AA 1 )-(AA 2 )- wherein -(AA 1 )- and -(AA 2 )- preferably have the meanings given above; • or simply a bivalent radical of an amino acid selected from the amino acids mentioned above; and Y is monosubstituted amino selected from lower alkylamino; octylamino; halonaphthyloxy- lower alkylamino or naphthyloxy-lower alkylamino; phenyl-lower alkylamino, di-phenyl-lower alkylamino, (mono- or di-halo-phenyl)-lower alkylamino, naphthalenyl-lower alkylamino, hydroxy-naphthalenyl-lower alkylamino or phenanthrenyl-lower alkylamino; cycloalkylamino; and cycloalkyl-lower alkylamino; or a salt thereof where at least one salt-forming group is present. 9. A compound of formula I according to claim 1 being selected from the following compounds: 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-lle-Asn-Gln-NH2 (SEQ ID NO: 1), 2-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2) (SEQ ID NO: 2), 1-(3-aminophenyl)ethyloxycarbonyl-Tyr(PO3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 4), 2-(4-methyl-5-thiazolyl)-ethyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 8), 2-(3-Hydroxyphenyl)ethyioxycarbonyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 9), 3-hydroxybenzyloxycarbonyl-Tyr(PO3H2)-lle-Asn-Gln-NH2 (SEQ ID NO: 10), 3,5-diaminobenzyloxycarbonyl-Tyr(PO3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 14), 3-(3-indole)propionoyl-Tyr(PO3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 15), 4-(N-acetylamino)phenoxyacetyl-Tyr(PO3H2)-lle-Asn-Gln-NH2 (SEQ ID NO: 17), 4-aminophenoxyacetyl-Tyr(PO3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 19), 3-aminophenoxyacetyl-Tyr(PO3H2)-lle-Asn-Gln-NH2 (SEQ ID NO: 20), 4-(3-indolyl)butyrolyl-Tyr(PO3H 2 )-lle-Asn-Gln-NH 2 (SEQ ID NO: 21), 3-indolyl-acetyI-Tyr(PO 3 H2)-He-Asn-Gln-NH2 (SEQ ID NO: 22), 2-amino-thiazol-4-yl-acetyl-Tyr(PO3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 26), 2,3-dihydrobenzofuran-5-carbonyl-Tyr(PO3H2)-lle-Asn-Gln-NH2 (SEQ ID NO: 28), 4-(N-methylamino)benzoyl-Tyr(Pθ3H 2 )-lle-Asn-Gln-NH2 (SEQ ID NO: 34), 3-aminobenzoyl-Tyr(PO3H2 . -lle-Asn-Gln-NH2 (SEQ ID NO: 40), quinoIine-6-carbonyl-Tyr(PO3H2)-lle-Asn-Gln-NH2 (SEQ ID NO: 41), 4-methoxycarbonylbenzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 42), 4-Amino-3-hydroxybenzoyl-Tyr(PO3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 46), 4-aminobenzoyl-Tyr(PO3H2)-lle-Asn-NH2 (SEQ ID NO: 50), 4-aminobenzoyl-Tyr(PO3H2)-lle-Asn-Gly-NH2 (SEQ ID NO: 53), 4-aminobenzoyl-Tyr(PO3H2)-lle-Asn-Val-NH2 (SEQ ID NO: 54), 4-aminobenzoyl-Tyr(PO3H2)-lle-Asn-Asp-NH2 (SEQ ID NO: 55), 4-aminobenzoyl-Tyr(PO3H2.-lle-Asn-Ac5C-NH2 (SEQ ID NO: 56), 4-aminobenzoyl-Tyr(PO3H2.-He-Asn-Asn-NH2 (SEQ ID NO: 57), or a pharmaceutically acceptable salt thereof if a salt forming group is present. 10. A compound of formula I according to claim 1 being selected from the following compounds: 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 3), 3-aminobenzyloxycarbonyl-Tyr(PO3H2)-Ac5C-Asn-Gln-NH2 (SEQ ID NO: 6), 3-aminobenzyloxycarbonyl-Tyr(PO3H2)-Ac6C-Asn-Gln-NH2 (SEQ ID NO: 7), 4-aminobenzoyl-Tyr(Pθ3H2)-He-Asn-Gln-NH2 (SEQ ID NO: 24), 4-aminobenzoyl-Tyr(PO3H2)-Asp-Asn-Gln-NH2 (SEQ ID NO: 51), 4-aminobenzoyl-Tyr(PO3H2)-Gly-Asn-Gln-NH2 (SEQ ID NO: 52), 4-aminobenzoyl-Tyr(Pθ3H2. -lle-Asn-βAla-NH2 (SEQ ID NO: 58), lndole-5-ylcarbonyl-Tyr(PO3H 2 )-lle-Asn-Gln-NH2 (SEQ ID NO: 61) lndole-5-ylcarbonyl-Tyr(PO3H2)-lle-Asn-NH2 (SEQ ID NO: 62) lndole-5-ylcarbonyl-Tyr(PO3-H2)-Ac6C-Asn-Gln-NH2 (SEQ ID NO: 63) 3-aminobenzyloxycarbonyl- -F2Pmp-lle-Asn-Gln-NH2 (SEQ ID NO: 64) and 4-(indole-3-yl)butyroyl-Tyr(PO 3 H 2 )-lle-Asn-GIn-NH 2 (SEQ ID NO: 67), or a pharmaceutically acceptable salt thereof if a salt-forming group is present. 11. A compound of formula I according to claim 1 being selected from the following compounds: trans-3,4-dihydroxy-cinnamoyl-Tyr(P03H2)-He-NH2 (SEQ ID NO: 70); trans-3,4-dihydroxy-cinnamoyl-Tyr(Pθ3H2)-Ac6C-NH2 (SEQ ID NO: 71); trans-3,4-dihydroxy-cinnamoyl-Tyr(P03H2)-Ac6C-Asn-NH2 (SEQ ID NO: 72) (very preferred); trans-3,4-dihydroxy-cinnamoyl-Tyr(P03H2)-Met-Asn-NH2 (SEQ ID NO: 74) (very preferred); 3-(3,4-dihydroxyphenyl)-propionyI-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 76); 3,4-dihydroxyphenyl-acetyl-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 77); trans-3,4-dihydroxy-cinnamoyl-Tyr(P03H2)-Ac7C-Asn-NH2 (SEQ ID NO: 80) (very preferred); trans-3,4-dihydroxy-cinnamoyl-Tyr(P03H2)-Nbo-Asn-NH2 (SEQ ID NO: 81) (very preferred); trans-3,4-dihydroxy-cinnamoyl-Tyr(Pθ3H2)-Nbo-NH2 (epimer 1) (SEQ ID NO: 82); trans-3,4-dihydroxy-cinnamoyl-Tyr(Pθ3H2)-Nbo-NH2 (epimer 2) (SEQ ID NO: 83); trans-4-hydroxy-cinnamoyl-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 84); 6-hydroxy-2-naphthoyl-Tyr(Pθ3H2)-He-NH2 (SEQ ID NO: 85); trans-3,4-dihydroxy-cinnamoyl-Tyr(P03H2)-Gln-NH2 (SEQ ID NO: 86); trans-3,4-dihydroxy-cinnamoyl-Tyr(Pθ3H2)-Glu-NH2 (SEQ ID NO: 87); 1-adamantoyl-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 95); cyclohexanoyl-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 96); succinamoyl-Tyr(Pθ3H2)-He-Asn-NH2 (SEQ ID NO: 103); trans-3,4-dihydroxy-cinnamoyl-Tyr(P03H2)-lle-Asn-NH2 (SEQ ID NO: 107) (very preferred); trans-3,4-dihydroxy-cinnamoyl-F 2 Pmp-lle-Asn-NH2 (SEQ ID NO: 111) (very preferred); trans-3,4-dihydroxy-cinnamoyl-F 2 Pmp-lle-NH2 (SEQ ID NO: 112); 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-Met-Asn-NH2 (SEQ ID NO: 113); indole-5-ylcarbonyl-L-F2Pmp-lle-Asn-NH2 (SEQ ID NO: 117) (very preferred); 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-Gln-Asn-NH2 (SEQ ID NO: 119) (very preferred); 3-Aminobenzyloxycarbonyl-Tyr(Pθ3H2)-Ac6C-Asn-NH2 (SEQ ID NO: 122) (very preferred); acetyl-Tyr(P03H2)-He-Asn-NH-(3-naphthalen-1 -yl-propyl) (SEQ ID NO: 123); acetyl-Tyr(Pθ3H2)-lle-Asn-NH-[3-(2-hydroxy-naphthalen-1-yl)-propyl] (SEQ ID NO: 124); acetyl-Tyr(P03H2)-lle-Asn-NH-(3-naphthalen-2-yl-propyl) (SEQ-ID-NO: 125); 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-lle-Asn-NH-(3-naphthalen-1 -yl-propyl) (SEQ ID NO: 142); 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-lle-Asn-NH-[3-(2-hydroxy-naphthalen-1-yl)-propyl] (SEQ ID NO: 143) (very preferred); 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-NH-(3-phenanthren-9-yl-propyl) (SEQ ID NO: 145); 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-He-Asn-NH-(3-methyl-butyl) (SEQ ID NO: 147); and 3-aminobenzyloxycarbonyl-Tyr(Pθ3H2)-lle-Asn-NH-cyclohexyl (SEQ ID NO: 148); or a pharmaceutically acceptable salt thereof if a salt-forming group is present. 12. lndole-5-ylcarbonyl-Tyr-lle-Asn-Gln-NH2 (SEQ ID NO: 114) of formula I acording to claim 1 , or a pharmaceutically acceptable salt thereof. 13. A pharmaceutical preparation comprising a compound of formula I, or a pharmaceutically acceptable salt thereof, according to any one of claims 1 to 12 and a pharmaceutically acceptable carrier material. 14. A compound of formula I, or a pharmaceutically acceptable salt thereof, according to any one of claims 1 to 12 for use in a method for the therapeutic or prophylactic treatment of the warm-blooded animal or human body. 15. The use of a compound of formula I, or a salt thereof, according to any one of claims 1 to 12 for the preparation of a pharmaceutical composition for the treatment of a disease that responds to inhibition of the interaction of a protein comprising an SH2 domain with a phosphoprotein. 16. A process for the preparation of a compound of formula I according to claim 1 , comprising reacting a fragment of a compound of formula I, which has a free carboxy group or a reactive derivative thereof, or, in the case of the introduction of X, a free carboxy or sulfo group, or a reactive derivative thereof, with a complementary fragment that has an amino group with at least one free hydrogen atom, or with a reactive derivative thereof, with formation of an amide bond; in the mentioned fragments free functional groups with the exception of those that participate in the reaction if required being present in protected form; and removing any protecting groups present; and, if desired, transforming a compound of formula I into a different compound of formula I; transforming a salt of an obtainable compound of formula I into the free compound or a different salt or an obtainable free compound of formula I into a salt; and/or separating obtainable mixtures of isomers of compounds of formula I into the individual isomers.

Inventors: CARAVATTI GIORGIO, FRETZ HEINZ, FURET PASCAL, GARCIA-ECHEVERRIA CARLOS, GAY BRIGITTE, RAHUEL JOSEPH, SCHOEPFER JOSEPH, CARAVATTI, GIORGIO, FRETZ, HEINZ, FURET, PASCAL, GARCIA-ECHEVERRIA, CARLOS, GAY, BRIGITTE, RAHUEL, JOSEPH, SCHOEPFER, JOSEPH
Applicants: CARAVATTI GIORGIO, CIBA GEIGY AG, FRETZ HEINZ, FURET PASCAL, GARCIA ECHEVERRIA CARLOS, GAY BRIGITTE, RAHUEL JOSEPH, SCHOEPFER JOSEPH, CARAVATTI, GIORGIO, CIBA-GEIGY AG, FRETZ, HEINZ, FURET, PASCAL, GARCIA-ECHEVERRIA, CARLOS, GAY, BRIGITTE, RAHUEL, JOSEPH, SCHOEPFER, JOSEPH
Application year: 1996
Main classification: C07K5
IPC codes: A61K38, C07K5, C07K14