PEPTIDE INHIBITORS OF INFLAMMATION

Abstract: Peptides derived from three regions of the lectin domain of GMP-140 and the related selectins, ELAM-1 and the lymphocyte homing receptor, have been found to inhibit neutrophil adhesion to GMP-140. These and additional peptides have been synthesized, having as their core region portions of the 23-30 amino acid sequence of GMP-140, with residue 1 defined as the N-terminus of the mature protein after the cleavage of the signal peptide. Examples demonstrate the inhibition of the binding of neutrophils to GMP-140 of peptides in concentrations ranging from 5 to 1500 mu M. It has been found that alterations within the core sequence, as well as N-terminal and C-terminal flanking regions, do not result in loss of biological activity. It has also been found that certain of these modifications can significantly increase the stability of peptides of Formula (I) or (II) against degradation by the enzymes found in human serum. The peptides are useful as diagnostics and, in combination with a suitable pharmaceutical carrier, for clinical applications in the modulation or inhibition of coagulation processes or inflammatory processes.

Description: PEPTIDE INHIBITORS OP INFLAMMATION Background of the Invention This invention is generally in the field of methods for the treatment and prevention of inflammatory responses using peptides derived from selectins including GMP-140, ELAM-1, and lymphocyte- homing receptor. The adherence of platelets and leukocytes to vascular surfaces is a critical component of the inflammatory response, and is part of a complex series of reactions involving the simultaneous and interrelated activation of the complement, coagulation, and immune systems. The complement proteins collectively play a leading role in the immune system, both in the identification and in the removal of foreign substances and immune complexes, as reviewed by Muller-Eberhard, H.J. , Ann. Rev. Biochem. 57:321-347 (1988) . Central to the complement system are the C3 and C4 proteins, which when activated covalently attach to nearby targets, marking them for clearance. In order to help control this process, a remarkable family of soluble and membrane-bound regulatory proteins has evolved, each of which interacts with activated C3 and/or C4 derivatives. The coagulation and inflammatory pathways are regulated in a coordinate fashion in response to tissue damage. For example, in addition to becoming adhesive for leukocytes, activated endothelial cells express tissue factor on the cell surface and decrease their surface expression of thro bomodulin, leading to a net facilitation of coagulation reactions on the cell surface. In some cases, a single receptor can be involved in both inflammatory and coagulation processes. Leukocyte adherence to vascular endothelium is a key initial step in migration of leukocytes to tissues in response to microbial invasion. Although a class of inducible leukocyte receptors, the CD11-CD18 molecules, are thought to have some role in adherence to endothelium, mechanisms of equal or even greater importance for leukocyte adherence appear to be due to inducible changes in the endothelium itself. Activated platelets have also been shown to interact with both neutrophils and monocytes in vitro. The interaction of platelets with monocytes may be mediated in part by the binding of thrombospondin to platelets and monocytes, although other mechanisms have not been excluded. The mechanisms for the binding of neutrophils to activated platelets are not well understood, except that it is known that divalent cations are required. In response to vascular injury, platelets are known to adhere to subendothelial surfaces, become activated, and support coagulation. Platelets and other cells may also play an important role in the recruitment of leukocytes into the wound in order to contain microbial invasion. Endothelium exposed to "rapid" activators such as thrombin and hista ine becomes adhesive for neutrophils within two to ten minutes, while endothelium exposed to cytokines such as tumor necrosis factor and interleukin-1 becomes adhesive after one to six hours. The rapid endothelial- dependent leukocyte adhesion has been associated with expression of the lipid mediator platelet activating factor (PAF) on the cell surface, and presumably, the appearance of other endothelial surface receptors. The slower cytokine-inducible endothelial adhesion for leukocytes is mediated, at least in part, by an endothelial cell receptor, ELAM-1, that is synthesized by endothelial cells after exposure to cytokines and then transported to the cell surface, where it binds neutrophils. The isolation, characterization and cloning of ELAM-1 is reviewed by Bevilacqua, et al., in Science 243, 1160-1165 (1989). A peripheral lymph node homing receptor, also called "the murine Mel 14 antigen", "Leu 8", the "Leu 8 antigen" and "LAM-1", is another structure on neutrophils, monocytes, and lymphocytes that binds lymphocytes to high endothelial venules in peripheral lymph nodes. The characterization and cloning of this protein is reviewed by Lasky, et al.. Cell 56, 1045-1055 (1989) (mouse) and Tedder, et al., J. Exp. Med. 170, 123-133 (1989). * GMP-140 (granule membrane protein 140) , also known as PADGEM, is a cysteine-rich and heavily glycosylated integral membrane glycoprotein with an apparent molecular weight of 140,000 as assessed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) . GMP-140 was first purified from human platelets by McEver and Martin, J. Biol. Chem. 259:9799-9804 (1984). The protein is present in alpha granules of resting platelets but is rapidly redistributed to the plasma membrane following platelet activation, as reported by Stenberg, et al., (1985) . The presence of GMP-140 in endothelial cells and its biosynthesis by these cells was reported by McEver, et al., Blood 70(5) Suppl. 1:355a, Abstract No. 1274 (1987). In endothelial cells, GMP-140 is found in storage granules known as the eibel-Palade bodies. (McEver, et al. J. Clin. Invest. 84:92-99 (1989) and Hattori, et al., J. Biol. Chem. 264:7768- 7771 (1989)). GMP-140 (called PADGEM) has also been reported to mediate the interaction of activated platelets with neutrophils and monocytes by Larsen, et al., in Cell 59, 305-312 (October 1989) and Hamburger and McEver, Blood 75:550-554 (1990). The cDNA-derived amino acid sequence, reported by Johnston, et al., in Cell 56, 1033-1044 (March 24 1989), and in U.S. Serial No. 07/320,408 filed March 8, 1989, indicates that it contains a number of modular domains that are likely to fold independently. Beginning at the N-terminus, these include a "lectin" domain, an "EGF" domain, nine tandem consensus repeats similar to those in complement binding proteins, a transmembrane domain (except in a soluble form that appears to result from differential splicing) , and a cytoplasmic tail. When platelets or endothelial cells are activated by mediators such as thrombin, the membranes of the storage granules fuse with the plasma membrane, the soluble contents of the granules are released to the external environment, and membrane bound GMP-140 is presented within seconds on the cell surface. The rapid redistribution of GMP-140 to the surface of platelets and endothelial cells as a result of activation suggested that this glycoprotein could play an important role at sites of inflammation or vascular disruption. This important role has been confirmed by the observation that GMP-140 is a receptor for neutrophils (Geng et al.. Nature 343:757-760 (1990); Hamburger and McEver, Blood 75:550-554 (1990)), monocytes (Larsen, et al. Cell 59:305-312 (1989); Moore, et al., J. Cell Biol. 112:491-499 (1991)), and a subset of lymphocytes (Moore, et al. J. Cell Biol. 112:491-499 (1991) and Moore, et al., Blood (Suppl 1) 78:439a (1991)). Thus, GMP-140 can serve as a receptor for leukocytes following its rapid mobilization to the surfaces of platelets and endothelial cells stimulated with agonists such as thrombin. This role in leukocyte recruitment may be important in hemostatic and inflammatory processes in both physiologic and pathologic states. Peptides derived from GMP-140 are described in U.S. Serial No. 07/554,199 entitled "Functionally Active Selectin-Derived Peptides" filed July 17, 1990 by Rodger P. McEver that are useful in diagnostics and in modulating the hemostatic and inflammatory responses in a patient wherein a therapeutically effective amount of a peptide capable of blocking leukocyte recognition of GMP-140 is administered to the patient. U.S. Serial No. 07/554,199 filed July 17, 1990 also discloses that peptide sequences within the lectin domain of GMP-140, having homology with the lectin domains of other proteins, especially ELAM-1 and the homing receptor, selectively inhibit neutrophil adhesion to purified GMP-140, and can therefore be used in diagnostic assays of patients and diseases characterized by altered binding by these molecules, in screening assays for compounds altering this binding, and in clinical applications to inhibit or modulate interactions of leukocytes with platelets or endothelial cells involving coagulation and/or inflammatory processes. ELAM-1, the homing receptor, and GMP-140 have been termed "selectins", based on their related structure and function. ELAM-1 is not present in unstimulated endothelium. However, when endothelium is exposed to cytokines such as tumor necrosis factor or interleukin-1, the gene for ELAM-1 is transcribed, producing RNA which in turn is translated into protein. The result is that ELAM-1 is expressed on the surface of endothelial cells one to four hours after exposure to cytokines, as reported by Bevilacqua et al., Proc.Natl.Acad.Sci.USA 84:9238-9242 (1987) (in contrast to GMP-140, which is stored in granules and presented on the cell surface within seconds after activation) . ELAM-1 has been shown to mediate the adherence of neutrophils to cytokine-treated endothelium and thus appears to be important in allowing leukocytes to migrate across cytokine- stimulated endothelium into tissues. The cDNA-derived primary structure of ELAM-1 indicates that it contains a "lectin" domain, an EGF domain, and six (instead of the nine in GMP-140) repeats similar to those of complement-regulatory proteins, a transmembrane domain, and a short cytoplasmic tail. There is extensive sequence homology between GMP-140 and ELAM- 1 throughout both proteins, but the similarity is particularly striking in the lectin and EGF domains. Homing receptors are lymphocyte surface structures that allow lymphocytes to bind to specialized endothelial cells in lymphatic tissues, termed high endothelial cells or high endothelial venules (reviewed by Yednock and Rose, Advances in Immunology, vol. 44, F.I. Dixon,ed., 313-378 (Academic Press, New York 1989) . This binding allows lymphocytes to migrate across the endothelium into the lymphatic tissues where they are exposed to processed antigens. The lymphocytes then re-enter the blood through the lymphatic system. The homing receptor contains a lectin domain, an EGF domain, two complement-binding repeats, a transmembrane domain, and a short cytoplasmic tail. The homing receptor also shares extensive sequence homology with GMP-140, particularly in the lectin and EGF domains. Based on a comparison of the lectin domains between GMP-140, ELAM-1, and the homing receptor (LEU- 8) , it may be possible to select those peptides inhibiting binding of neutrophils to GMP-140 which will inhibit binding of ELAM-1, the homing receptor, and other homologous selectins, to components of the inflammatory process, or, conversely, which will inhibit only GMP-140 binding. The in vivo significance of platelet-leukocyte interactions has not been studied carefully. However, in response to vascular injury, platelets are known to adhere to subendothelial surfaces, become activated, and support coagulation. Platelets and other cells may also play an important role in the recruitment of leukocytes into the wound in order to contain microbial invasion. Conversely, leukocytes may recruit platelets into tissues at sites of inflammation, as reported by Issekutz, et al., Lab. Invest. 49:716 (1983). The coagulation and inflammatory pathways are regulated in a coordinate fashion in response to tissue damage. For example, in addition to becoming adhesive for leukocytes, activated endothelial cells express tissue factor on the cell surface and decrease their surface expression of thro bomodulin, leading to a net facilitation of coagulation reactions on the cell surface. In some cases, a single receptor can be involved in both inflammatory and coagulation processes. Proteins involved in the he ostatic and inflammatory pathways are of interest for diagnostic purposes and treatment of human disorders. However, there are many problems using proteins therapeutically. Proteins are usually expensive to produce in quantities sufficient for administration to a patient. Moreover, there can be a reaction against the protein after it has been administered more than once to the patient. It is therefore desirable to develop peptides having the same, or better, activity as the protein, which are inexpensive to synthesize, reproducible and relatively innocuous. It is preferable to develop peptides which can be prepared synthetically, having activity at least equal to, or greater than, the peptides derived from the protein itself. It is therefore an object of the present invention to provide peptides interacting with cells recognized by selectins, including GMP-140, ELAM-1, and lymphocyte homing receptor. It is another object of the present invention to provide methods for using these peptides to inhibit leukocyte adhesion to endothelium or to platelets. It is a further object of the present invention to provide methods for using these peptides to modulate the immune response and the hemostatic pathway. It is yet another object of the present invention to provide peptides for use in diagnostic assays relating to GMP-140, ELAM-1, and lymphocyte homing receptor. Summary of the Invention Peptides derived from three regions of the lectin domain of GMP-140 and the related selectins, ELAM-1 and the lymphocyte homing receptor, have been found to inhibit neutrophil adhesion to GMP-140. These and additional peptides have been synthesized having the following formulae: R 1 -X-P-Q-S-T-U-V-W-Z-Y-R 2 (I) R X -P-Q-S-T-U-V-W-Z-R 2 (II) or a pharmaceutically acceptable salt thereof, wherein: X in Formula (I) and P in Formula (II) are the N-terminus amino acids, and R 1 is a moiety attached to the function (NHR 1 ) , Y in Formula (I) and Z in Formula (II) are the C-terminus amino acids, and R is the moiety attached to the singly-bonded oxygen in the carboxy function (C(O)OR 2 ), P is D- or L-tyrosine, D- or L-phenylalanine, D- or L-lysine, D- or L-glutamic acid, D- or L-arginine, D- or L-cysteine, D- or L- O-R 3 -tyrosine, D- or L-N α - R 3 -tyrosine, D- or L-4-amino phenylalanine, D- or L- R 4 -phenylalanine, D- or L-pyridylalanine, D- or L- naphthylalanine, or D- or L-tetrahydroisoquinoline carboxylic acid, where R 3 is lower alkyl or aryl and R 4 is halogen (fluorine, chlorine, bromine or iodine) , Q is D- or L-threonine, D- or L-lysine, D- or L- glutamic acid, D- or L-cysteine, or glycine, S is D- or L-aspartic acid, D- or L-histidine, D- or L-glutamic acid, D- or L-asparagine, D or L- glutamine, D- or L-alanine, D- or L-phenylalanine, D- or L-lysine, or glycine, T, U, V and W are independently D- or L-leucine, D- or L-isoleucine, D- or L-alanine, D- or L-valine, D- or L-alloisoleucine, glycine, D- or L-glutamic acid, D- or L-aspartic acid, D- or L-asparagine, D- or L-glutamine, D- or L-threonine, or desamino acid where desamino acid refers to the deletion of either residues T, U, V, or W from the peptide formulas I or II, Z is D- or L-glutamine, D- or L-glutamic acid and D- or L-asparagine, R 1 is H (signifying a free N-terminal group) , formyl, lower alkanoyl, aroyl or desamino (meaning the amino acid adjacent to the group R 1 , either X in formula I or P in formula 2 lacks the α-amino group of the amino acid, and is replaced with H) , R is H (signifying in a free C-terminal carboxylic acid), O(lower alkyl), O(aryl), NR 3 R 4 where R 3 and R 4 are independently H or lower alkyl, or descarboxy (meaning the α-carboxylic acid group of the amino acid to which R 1 is adjacent in formula I or 2, Y or Z, respectively, is replaced with H) , X and Y are linear chains of from one to ten amino acids. Peptides of the Formula I and II have as their core region portions of the 23-30 amino acid sequence of GMP-140, with residue 1 defined as the N-terminus of the mature protein after the cleavage of the signal peptide. Examples demonstrate the inhibition of the binding of neutrophils to GMP-140 of peptides of Formula I or II in concentrations ranging from 5 to 1500 μM. It has been found that alterations within the core sequence, as well as N-terminal and C- terminal flanking regions, do not result in loss of biological activity. It has also been found that certain of these modifications can significantly increase the stability of peptides of Formula I or II against degradation by the enzymes found in human } - serum. The peptides are useful as diagnostics and, in combination with a suitable pharmaceutical carrier, for clinical applications in the modulation or inhibition of coagulation processes or inflammatory processes. Brief Description of the Drawings Figure 1 shows the activity of several peptides of Formulas I and II in inhibiting the binding of neutrophils to GMP-140, % inhibition versus concentration of peptide (mM) , (dark squares, Cys- Gln-Asn-Arg-Tyr-Thr-Asp-Leu-Val-Ala-Ile-Gln-a ide; open square, Asn-Arg-Tyr-Thr-Asp-Leu-Val-Ala-Ile-Gln- a ide; dark diamond, Arg-Tyr-Thr-Asp-Leu-Val-Ala-Ile- Gln-amide; open diamond, Tyr-Thr-Asp-Leu-Val-Ala-Ile- Gln-amide; dark triangle, Acetyl-Tyr-Thr-Asp-Leu-Val- Ala-Ile-Gln-amide; open triangle, Tyr-Thr-Glu-Leu- Val-Ala-Ile-Gln-amide; X, Tyr-Thr-His-Leu-Val-Ala- Ile-Gln-amide; *, Tyr-Thr-Asp-Leu-Val-Ala-Ile-Gln- Asn-Lys-Asn-Glu-amide; —, Leu-Gln-Thr-Ala-Tyr-Asp- Val-Ile-amide (negative control) ) . Figure 2 shows the significant increase in stability against enzymes found in human serum that can be achieved by the modifications set down in Formula I and II, graphing percent of peptide remaining versus time (minutes) (dark triangle, Ac- YTDLVAIQ-NH 2 , 0, YTDLVAIQ-NH 2 ) . Detailed Description of the Invention Peptides having GMP-140-like activity, therapeutic compositions containing these peptides, methods for the preparation of these peptides and methods for use thereof, are disclosed. These peptides have either of the following formulas: R 1 -X-P-Q-S-T-U-V-W-Z-Y-R 2 (I) R 1 -P-Q-S-T-U-V-W-Z-R 2 (II) or a pharmaceutically acceptable salt thereof, wherein: X in Formula (I) and P in Formula (II) are the N-terminus amino acids, and R is a moiety attached to the amine function (NHR 1 ) , Y in Formula (I) and Z in Formula (II) are the C-terminus amino acids, and R 2 is the moiety attached to the singly-bonded oxygen in the carboxy function (C(O)OR 2 ), P is D- or L-tyrosine, D- or L-phenylalanine, D- or L-lysine, D- or L-glutamic acid, D- or L-arginine, D- or L-cysteine, D- or L- O-R -tyrosine, D- or L-N - R -tyrosine, D- or L-4-amino phenylalanine, D- or L- R -phenylalanine, D- or L-pyridylalanine, D- or L- naphthylalanine, or D- or L-tetrahydroisoquinoline carboxylic acid, where R 3 is lower alkyl or aryl and R is halogen (fluorine, chlorine, bromine or iodine) , Q is D- or L-threonine, D- or L-lysine, D- or L- glutamic acid, D- or L-cysteine, or glycine, S is D- or L-aspartic acid, D- or L-histidine, D- or L-glutamic acid, D- or L-asparagine, D or L- glutamine, D- or L-alanine, D- or L-phenylalanine, D- or L-lysine, or glycine, T, U, V and W are independently D- or L-leucine, D- or L-isoleucine, D- or L-alanine, D- or L-valine, D- or L-alloisoleucine, glycine, D- or L-glutamic acid, D- or L-aspartic acid, D- or L-asparagine, D- or L-glutamine, D- or L-threonine, or desamino acid where desamino acid refers to the deletion of either residues T, U, V, or W from the peptide formulas I or II, Z is D- or L-glutamine, D- or L-glutamic acid and D- or L-asparagine, R 1 is H (signifying a free N-terminal group) , formyl, lower alkanoyl, aroyl or desamino (meaning the amino acid adjacent to the group R 1 , either X in formula I or P in formula 2 lacks the α-amino group of the amino acid, and is replaced with H) , R 2 is H (signifying in a free C-terminal carboxylic acid), 0(lower alkyl), O(aryl), NR 3 R 4 where R 3 and R 4 are independently H or lower alkyl, or descarboxy (meaning the o;-carboxylic acid group of the amino acid to which R 1 is adjacent in formula I or 2, Y or Z, respectively, is replaced with H) , X and Y are linear chains of from one to ten amino acids. Preferred peptides are those of Formula I wherein R 1 is H and R 2 is NR 3 R 4 , and Formula II wherein R 1 is H or acetyl and R 1 is NR 3 R 4 , wherein S is aspartic acid, glutamic acid or histidine. Most preferred peptides are Tyr-Thr-Asp-Leu- Val-Ala-Ile-Gln-NH 2 ; Tyr-Thr-His-Leu-Val-Ala-Ile-Gln- NH 2 ; Acetyl-Tyr-Thr-Asp-Leu-Val-Ala-Ile-Gln-NH 2 ; Cys- Gln-Asn-Arg-Tyr-Thr-Asp-Leu-Val-Ala-Ile-Gln-NH 2 ; Asn- Arg-Tyr-Thr-Asp-Leu-Val-Ala-Ile-Gln-NH 2 ; Arg-Tyr-Thr- Asp-Leu-Val-Ala-Ile-Gln-NH 2 ; Tyr-Thr-Glu-Leu-Val-Ala- Ile-Gln-NH 2 ; Tyr-Thr-Asp-Leu-Val-Ala-Ile-Gln-Asn-Lys- Asn-Glu-NH 2 ; D-Tyr-Thr-Asp-Leu-Val-Ala-Ile-Gln-NH 2 ; Tyr-D-Thr-Asp-Leu-Val-Ala-Ile-Gln-NH 2 ; Tyr-Thr-D-Asp- Leu-Val-Ala-Ile-Gln-NH 2 ; Phe-Thr-Asp-Leu-Val-Ala-Ile- Gln-NH 2 ; Tyr-Thr-D-Asp-Leu-Val-Ala-Ile-Gln-NH 2 ; Tyr- Thr-Asp-Leu-Val-Ala-D-Ile-Gln-NH 2 ; Tyr-Thr-Asp-Ala- Val-Ala-Ile-Gln-NH 2 ; Tyr-Thr-Ala-Leu-Val-Ala-Ile-Gln- NH 2 ; Tyr-Thr-Phe-Leu-Val-Ala-Ile-Gln-NH 2 ; Tyr-Thr-Lys- Leu-Val-Ala-Ile-Gln-NH 2 ; Lys-Thr-Asp-Leu-Val-Ala-Ile- Gln-NH 2 ; Gln-Asn-Arg-Tyr-Thr-Asp-Leu-Val-Ala-Ile-Gln- NH 2 ; Asn-Arg-Tyr-Thr-Asp-Leu-Val-Ala-Ile-Gln-NH 2 ; Arg- Gly-His-Leu-Val-Ala-Ile-Gln-NH 2 ; and Arg-Gly-Asp-Leu- Val-Ala-Ile-Gln-NH 2 . As used herein, the term "lower alkyl" includes branched, straight-chain, and cyclic saturated hydrocarbons having from one to six carbon atoms, such as methyl, ethyl, propyl, isopropyl, butyl, isobutyl, t-butyl, pentyl, isopentyl, neopentyl, and hexyl. The term "lower alkanoyl" means RC(O) , wherein R a lower alkyl group. The term aroyl means where ArC(O) , wherein Ar is an aryl group, an aromatic or heteroaromatic structure having between one and three rings, which may or may not be ring fused structures, and are optimally substituted with halogens, carbons, or other heteroato s such as nitrogen (N) , sulfur (S) , phosphorus (P) , and boron (B) . The peptides of formula I can be used in the form of the free peptide or a pharmaceutically acceptable salt. Amine salts can be prepared by mixing the peptide with an acid according to known methods. Suitable acids include inorganic acids such as hydrochloric acid, hydrobromic acid, perchloric acid, nitric acid, thiocyanic acid, sulfuric acid, and phosphoric acid, and organic acids such as formic acid, acetic acid, propionic acid, glycolic acid, lactic acid, pyruvic acid, oxalic acid, malonic acid, succinic acid, maleic acid, fumaric acid, anthranilic acid, cinnamic acid, naphthalenesulfonic acid, and sulfanilic acid. Carboxylic acid groups in the peptide can be converted to a salt by mixing the peptide with a base according to known methods. Suitable bases include inorganic bases such as sodium hydroxide, ammonium hydroxide, and potassium hydroxide, and organic bases such as mono-, di-, and tri-alkyl and aryl amines (e.g., triethylamine, disopropyla ine, methylamine, and dimethylamine and optionally substituted mono-, di, and tri-ethanolamines. As referred to herein, the amino acid components of the peptides and certain materials used in their preparation are identified by abbreviations for convenience. These abbreviations are as follows: Reagents Abbreviations Trifluoroacetic acid TFA Methylene chloride CH 2 C1, N,N-Diisopropylethylamine DIEA N-Methylpyrrolidone NMP 1-Hydroxybenzotriazole HOBT Dimethylsulfoxide DMSO Acetic anhydride Ac 2 ° Methods of Preparation of Peptides The peptides can generally be prepared following known techniques, as described for example in the cited publications, the teachings of which are specifically incorporated herein. In a preferred method, the peptides are prepared following the solid- phase synthetic technique initially described by Merrifield in J.Amer.Chem.Soc. , 85, 2149-2154 (1963) . Other techniques may be found, for example, in M. Bodanszky, et al., Peptide Synthesis, second edition, (John Wiley & Sons, 1976) , as well as in other reference works known to those skilled in the art. Appropriate protective groups usable in such syntheses and their abbreviations will be found in the above text, as well as in J.F.W. McOmie, Protective Groups in Organic Chemistry. (Plenum Press, New York, 1973) . The common protective groups used herein are t-butyloxycarbonyl (Boc) , fluorenylmethoxycarbonyl (FMOC) , benzyl (Bzl) , tosyl (Tos) , o-bromo- phenylmethoxycarbonyl (BrCBZ) , phenylmethoxycarbonyl (CBZ) , 2-chloro-phenylmethoxycarbonyl, (2-C1-CBZ) , 4- methoxy-2,3,6-trimethylbenzenesulfonyl (Mtr), trityl (Trt) , formyl (CHO) , and tertiary butyl (t-Bu) . General synthetic procedures for the synthesis of peptides of Formula I and II by solid phase methodology are as follows: A. General Synthetic Procedures for Solid Phase Peptide Synthesis Using ϊ -Boc Protection. ONS TIME B. General Synthetic Procedure For Solid Phase Peptide synthesis Using N**- FMOC Protection REPETITIONS TIME 1. 20% piperdine in NMP 2. 20% piperdine in NMP 3. NMP 4. Coupling Preformed FMOC-Amino Acid- HOBT active ester in NMP 5. NMP 6 7 min N-terminal acetylation on the deprotected N α - amino group of peptides synthesized using either Boc or FMOC strategies is accomplished with 10% Ac 2 0 and 5% DIEA in NMP, followed by washing of the peptide resin with NMP and/or CH 2 C1 2 . The peptides can also be prepared using standard genetic engineering techniques known to those skilled in the art. For example, the peptide can be produced enzymatically by inserting nucleic acid encoding the peptide into an expression vector, expressing the DNA, and translating the DNA into the peptide in the presence of the required amino acids. The peptide is then purified using chromatographic or electrophoretic techniques, or by means of a carrier protein which can be fused to, and subsequently cleaved from, the peptide by inserting into the expression vector in phase with the peptide encoding sequence a nucleic acid sequence encoding the carrier protein. The fusion protein-peptide may be isolated using chromatographic, electrophoretic or immunological techniques (such as binding to a resin via an antibody to the carrier protein) . The peptide can be cleaved using chemical methodology or enzymatically, as by, for example, hydrolases. Methods of Preparation of Pharmaceutical Compositions To prepare the pharmaceutical compositions containing these peptides, a peptide of Formula I or II or a base or acid addition salt thereof is combined as the active ingredient with a pharmaceutical carrier according to conventional pharmaceutical compounding techniques. This carrier may take a wide variety of forms depending on the form of preparation desired for administration, e.g., sublingual, rectal, nasal, oral, or parenteral. In preparing the compositions in oral dosage form, any of the usual pharmaceutical media may be employed, for example, water, oils, alcohols, flavoring agents, preservatives, and coloring agents, to make an oral liquid preparation (e.g., suspension, elixir, or solution) or with carriers such as starches, sugars, diluents, granulating agents, lubricants, binders, and disintegrating agents, to make an oral solid preparation (e.g., powder, capsule, or tablet) . Controlled release forms or enhancers to increase bioavailability may also be used. Because of their ease in administration, tablets and capsules represent the most advantageous oral dosage unit form, in which case solid pharmaceutical carriers are employed. If desired, tablets may be sugar coated or enteric coated by standard techniques. For parenteral products, the carrier will usually be sterile water, although other ingredients to aid solubility or as preservatives may be included. Injectable suspensions may also be prepared, in which case appropriate liquid carriers and suspending agents can be employed. The peptides can also be administered locally at a wound or inflammatory site by topical application of a solution or cream. Alternatively, the peptide may be administered in liposomes or microspheres (or microparticles) . Methods for preparing liposomes and microspheres for administration to a patient are known to those skilled in the art. U.S. Patent No. 4,789,734 describe methods for encapsulating biological materials in liposomes. Essentially, the material is dissolved in an aqueous solution, the appropriate phospholipids and lipids added, along with surfactants if required, and the material dialyzed or sonicated, as necessary. A good review of known methods is by G. Gregoriadis, Chapter 14. "Liposomes", Drug Carriers in Biology and Medicine pp. 287-341 (Academic Press, 1979) . Microspheres formed of polymers or proteins are well known to those skilled in the art, and can be tailored for passage through the gastrointestinal tract directly into the bloodstream. Alternatively, the peptide can be incorporated and the microspheres, or composite of microspheres, implanted for slow release over a period of time, ranging from days to months. See, for example, U.S. Patent No. 4,906,474, 4,925,673, and 3,625,214. Methods for Demonstrating Binding Peptides that are biologically active are those which inhibit binding of neutrophils, monocytes, subsets of lymphocytes or other cells to GMP-140, or which inhibit leukocyte adhesion to endothelium that is mediated by ELAM-1 and/or the homing receptor. Peptides can be screened for their ability to inhibit adhesion to cells, for example, neutrophil adhesion to purified GMP-140 immobilized on plastic wells, using the assay described by Geng, et al.. Nature 343. 757-760 (1990). Human neutrophils are isolated from heparinized whole blood by density gradient centrifugation on f Mono-Poly resolving media, Flow Laboratories. Neutrophil suspensions are greater than 98% pure and greater than 95% viable by trypan blue exclusion. For adhesion assays, neutrophils are suspended at a concentration of 2 x 10 6 cells/ml in Hanks 7 balanced salt solution containing 1.26 mM Ca 2+ and 0.81 mM Mg 2+ (HBSS, Gibco) with 5 mg/ml human serum albumin (HBSS/HSA) . Adhesion assays are conducted in triplicate in 96-well microtiter plates, Corning, incubated at 4°C overnight with 50 microliters of various protein solutions. GMP-140 is isolated from human platelet lysates by immunoaffinity chromatography on antibody S12- Sepharose™ and ion-exchange chromatography on a Mono- Q column (FLPC, Pharmacia Fine Chemicals) , as follows. Outdated human platelet packs (100 units) obtained from a blood bank and stored at 4°C are pooled, adjusted to 5 mM EDTA at pH 7.5, centrifuged at 4,000 rpm for 30 min in 1 liter bottles, then washed three times with 1 liter of 0.1 M NaCl, 20 mM Tris pH 7.5 (TBS), 5 mM EDTA, 5 mM benzamidine. The pellets are then resuspended in a minimum amount of wash buffer and made 1 mM in DIFP, then frozen in 50 ml screwtop tubes at -80°C. The frozen platelets are thawed and resuspended in 50 ml TBS, 5 mM benzamidine, 5 mM EDTA pH 7.5, 100 M leupeptin. The suspension is frozen and thawed two times in a dry ice-acetone bath using a 600 ml lyophilizing flask, then homogenized in a glass/teflon mortar and pestle and made 1 mM in DIFP. The NaCl concentration is adjusted to 0.5 M with a stock solution of 4 M NaCl. After stirring the suspension at 4°C, it is centrifuged in polycarbonate tubes at 33,000 rpm for 60 min at 4°C. The supernatant (0.5 M NaCl wash) is removed and saved; this supernatant contains the soluble form of GMP-140. Care is taken not to remove the top part of the pellet with the supernatant. The pellets are then homogenized in extraction buffer (TBS, 5 mM benzamidine, 5 mM EDTA, pH 7.5, 100 μM leupeptin, 2% Triton X-100) . After centrifugation at 19,500 rpm for 25 min at 4°C, the supernatant is removed. The extraction procedure is repeated with the pellet and the supernatant is combined with the first supernatant. The combined extracts, which contain the membrane form of GMP-140, are adjusted to 0.5 M NaCl. The soluble fraction (0.5 M NaCl wash) and the membrane extract (also adjusted to 0.5 M NaCl) are absorbed with separate pools of the monoclonal antibody S12 (directed to human GMP-140) previously coupled to Affigel (Biorad) at 5 mg/ml for 2 h at 4°C. After letting the resins settle, the supernatants are removed. The S12 Affigel containing bound GMP-140 is then loaded into a column and washed overnight at 4°C with 400 ml of 0.5 M NaCl, 20 mM Tris pH 7.5, 0.01% Lubrol PX. Bound GMP-140 is eluted from the S12 Affigel with 100 ml of 80% ethylene glycol, 1 mM MES pH 6.0, 0.01% Lubrol PX. Peak fractions with absorbance at 280 nm are pooled. Eluates are dialyzed against TBS with 0.05% Lubrol, then applied to a Mono Q column (FPLC from Pharmacia) . The concentrated protein is step eluted with 2 M NaCl, 20 mM Tris pH 7.5 (plus 0.05% Lubrol PX for the membrane fraction). Peak fractions are dialyzed into TBS pH 7.5 (plus 0.05% Lubrol PX for the membrane fraction) . GMP-140 is plated at 5 micrograms/ml and the control proteins: human serum albumin (Alb) , platelet glycoprotein Hb/IIIa (lib) , von Willebrand factor (vWF) , fibrinogen (FIB) , thrombomodulin (TM) , gelatin (GEL) or human serum (HS) , are added at 50 micrograms/ml. All wells are blocked for 2 h at 22°C with 300 microliters HBSS containing 10 mg/ml HSA, then washed three times with HBSS containing 0.1% Tween-20 and once with HBSS. Cells (2 x 10 5 per well are added to the wells and incubated at 22°C for 20 min. The wells are then filled with HBSS/HSA, sealed with acetate tape (Dynatech) , and centrifuged inverted at 150 g for 5 min. After discarding nonadherent cells and supernates, the contents of each well are solubilized with 200 microliters 0.5% hexadecyltrimethylammonium bromide, Sigma, in 50 mM potassium phosphate, pH 6.0, and assayed for myeloperoxidase activity, Ley, et al., Blood 73, 1324- 1330 (1989) . The number of cells bound is derived from a standard curve of myeloperoxidase activity versus numbers of cells. Under all assay conditions, the cells release less than 5% of total myeloperoxidase and lactate dehydrogenase. Inhibition is read as a lower percent adhesion, so that a value of 5% means that 95% of the specific adhesion was inhibited. Clinical Applications. The subject peptides are generally active when administered parenterally in amounts above about 1 μg peptide/kg of body weight. For treatment to prevent organ injury in cases involving reperfusion, the peptides may be administered parenterally from about 0.01 to about 10 mg peptide/kg body weight. Generally, the same range of dosage amounts may be used in treatment of the other diseases or conditions where inflammation is to be reduced. This dosage will be dependent, in part, on whether one or more peptides are administered. A synergistic effect may be seen with combinations of peptides from different, or overlapping, regions of the lectin domain, or in combination with peptides derived from the EGF domain of GMP-140. Since the selectins have several functions related to leukocyte adherence, inflammation, and coagulation, clinically, compounds which interfere with binding of GMP-140, ELAM-1 or LEU-8 can be used to modulate these responses. For example, the peptides can be used to competitively inhibit leukocyte adherence by competitively binding to GMP-140 receptors on the surface of leukocytes. This kind of therapy would be particularly useful in acute situations where effective, but transient, inhibition of leukocyte- mediated inflammation is desirable. Chronic therapy by infusion of the peptides may also be feasible in some circumstances. An inflammatory response may cause damage to the host if unchecked, because leukocytes release many toxic molecules that can damage normal tissues. These molecules include proteolytic enzymes and free radicals. Examples of pathological situations in which leukocytes can cause tissue damage include injury from ischemia and reperfusion, bacterial sepsis and disseminated intravascular coagulation, adult respiratory distress syndrome, tumor metastasis, rheumatoid arthritis and atherosclerosis. Reperfusion injury is a major problem in clinical cardiology. Therapeutic agents, that reduce leukocyte adherence in ischemic myocardium can significantly enhance the therapeutic efficacy of thrombolytic agents. Thrombolytic therapy with agents such as tissue plasminogen activator or streptokinase can relieve coronary artery obstruction in many patients with severe myocardial ischemia prior to irreversible myocardial cell death. However, many such patients still suffer myocardial neurosis despite restoration of blood flow. This "reperfusion injury" is known to be associated with adherence of leukocytes to vascular endothelium in the ischemic zone, presumably in part because of activation of platelets and endothelium by thrombin and cytokines that makes them adhesive for leukocytes (Romson et al., Circulation 67: 1016-1023, 1983). These adherent leukocytes can migrate through the endothelium and destroy ischemic myocardium just as it is being rescued by restoration of blood flow. There are a number of other common clinical disorders in which ischemia and reperfusion results in organ injury mediated by adherence of leukocytes to vascular surfaces, including strokes; mesenteric and peripheral vascular disease; organ transplantation; and circulatory shock (in this case many organs might be damaged following restoration of blood flow) . Bacterial sepsis and disseminated intravascular coagulation often exist concurrently in critically ill patients. They are associated with generation of thrombin, cytokines, and other inflammatory mediators, activation of platelets and endothelium, and adherence of leukocytes and aggregation of platelets throughout the vascular system. Leukocyte-dependent organ damage is an important feature of these conditions. Adult respiratory distress syndrome is a devastating pulmonary disorder occurring in patients with sepsis or following trauma, which is associated with widespread adherence and aggregation of leukocytes in the pulmonary circulation. This leads to extravasation of large amounts of plasma into the lungs and destruction of lung tissue, both mediated in large part by leukocyte products. Two related pulmonary disorders that are often fatal are in immunosuppressed patients undergoing allogeneic bone marrow transplantation and in cancer patients suffering from complications that arise from generalized vascular leakage resulting from treatment with interleukin-2 treated LAK cells (lymphokine- activated lymphocytes) . LAK cells are known to adhere to vascular walls and release products that are presumably toxic to endothelium. Although the mechanism by which LAK cells adhere to endothelium is not known, such cells could potentially release molecules that activate endothelium and then bind to endothelium by mechanisms similar to those operative in neutrophils. Tumor cells from many malignancies (including carcinomas, lymphomas, and sarcomas) can metastasize to distant sites through the vasculature. The mechanisms for adhesion of tumor cells to endothelium and their subsequent migration are not well understood, but may be similar to those of leukocytes in at least some cases. The association of platelets with metastasizing tumor cells has been well described, suggesting a role for platelets in the spread of some cancers. Platelet-leukocyte interactions are believed to be important in atherosclerosis. Platelets might have a role in recruitment of monocytes into atherosclerotic plaques; the accumulation of monocytes is known to be one of the earliest detectable events during atherogenesis. Rupture of a fully developed plaque may not only lead to platelet deposition and activation and the promotion of thrombus formation, but also the early recruitment of neutrophils to an area of ischemia. Another area of potential application is in the treatment of rheumatoid arthritis. The criteria for assessing response to therapeutic modalities employing these peptides are dictated by the specific condition and will generally follow standard medical practices. For example, the criteria for the effective dosage to prevent extension of myocardial infarction would be determined by one skilled in the art by looking at marker enzymes of myocardial necrosis in the plasma, by monitoring the electrocardiogram, vital signs, and clinical response. For treatment of acute respiratory distress syndrome, one would examine improvements in arterial oxygen, resolution of pulmonary infiltrates, and clinical improvement as measured by lessened dyspnea and tachypnea. For treatment of patients in shock (low blood pressure) , the effective dosage would be based on the clinical response and specific measurements of function of vital organs such as the liver and kidney following restoration of blood pressure. Neurologic function would be monitored in patients with stroke. Specific tests are used to monitor the functioning of transplanted organs; for example, serum creatinine, urine flow, and serum electrolytes in patients undergoing kidney transplantation. Diagnostic Reagents. The peptides can also be used for the detection of human disorders in which the ligands for the selectins might be defective. Such disorders would most likely be seen in patients with increased susceptibility to infections in which leukocytes might not be able to bind to activated platelets or endothelium. Cells to be tested, usually leukocytes, are collected by standard medically approved techniques and screened. Detection systems include ELISA procedures, binding of radiolabeled antibody to immobilized activated cells, flow cytometry, or other methods known to those skilled in the arts. Inhibition of binding in the presence and absence of the lectin domain peptides can be used to detect defects or alterations in selectin binding. For selectins, such disorders would most likely be seen in patients with increased susceptibility to infections in which leukocytes would have defective binding to platelets and endothelium because of deficient leukocyte ligands for GMP-140. The peptide is labeled radioactively, with a fluorescent tag, enzymatically, or with electron dense material such as gold for electron microscopy. The cells to be examined, usually leukocytes, are incubated with the labeled peptides and binding assessed by methods described above with antibodies to GMP-140, or by other methods known to those skilled in the art. If ligands for GMP-140 are also found in the plasma, they can also be measured with standard ELISA or radioimmunoassay procedures, using labeled GMP-140-derived peptide instead of antibody as the detecting reagent. The following examples are presented to illustrate the invention without intending to specifically limit the invention thereto. In the examples and throughout the specifications, parts are by weight unless otherwise indicated. EXAMPLE l: Preparation of Tyrosyl-threonyl-histidyl- leucyl-valyl-alanyl-isoleucyl-glutamine- a ide. The peptide was prepared on an ABI model 431A peptide synthesizer using Version 1.12 of the standard scale Boc software. The amino acids used were Boc- (BrCBZ)Tyr, Boc-(Bzl)Thr, Boc-(Tos)His, Boc-Leu, Boc- Val, Boc-Ala, Boc-Ile and Boc-Gln. 4- Methylbenzhydrylamine resin (0.625 g, 0.5 mmol) was used in the synthesis. The final weight of the resin was 1.13 g. The peptide was cleaved from the resin (1.03 g) using 11 mL of HF and l.l mL of anisole for 60 min at 0° C. The hydrogen fluoride was evaporated using a stream of nitrogen and the resulting mixture triturated with ether. The solids were removed by filtration and extracted with 25 mL of a 50% solution of TFA in methylene chloride. Removal of the resin by filtration, evaporation of the solvent and trituration of the residue with ether gave 0.52 g of crude peptide. The crude peptide (55 mg) was purified on a Vydac C-18 column (10 μ 2.2 x 25 cm), eluting with a gradient of 10 to 20% of acetonitrile in 0.1% aqueous TFA over 20 minutes at a flow rate of 8 mL per minute. Fractions were collected, analyzed by HPLC and pure fractions pooled and lyophilized to give 3.9 mg of purified peptide. Amino acid analysis: Ala 0.98 (1.0), Glx 1.02 (1.0), His 1.06 (1.0), He 1.07 (1.0), Leu 1.07 (1.0), Thr 0.85 (1.0), Tyr 0.85 (1.0), Val 0.94 (1.0). FAB/MS: MH + 944 (calcd 944). EXAMPLE 2: Preparation of Tyrosyl-threonyl-glutamyl- leucyl-valyl-alanyl-isoleucyl-glutamine- amide. The peptide was prepared on a ABI model 431A peptides synthesizer using Version 1.12 of the standard scale Boc software. The amino acids used were Boc-(BrCBZ)Tyr, Boc-(Bzl)Thr, Boc-(Bzl)Glu, Boc- Leu, Boc-Val, Boc-Ala, Boc-Ile, Boc-Gln. 4- methylbenzhydrylamine resin (0.625 g, 0.5 mmol) was used in the synthesis. Final weight of the resin was 1.20 g. The peptide was cleaved from the resin (1.10 g) using 11 mL of HF and 1.1 mL of anisole for 60 minutes at 0° C. The hydrogen fluoride was removed using a stream of dry nitrogen, the residue triturated with ether and the ether removed by filtration. The remaining solids were triturated with 25 mL of a 50% solution of TFA in methylene chloride. The resin was removed by filtration, the solution evaporated under reduced pressure and the residue triturated with ether to give 0.40 g of the crude peptide, isolated by filtration. The crude peptide (0.31 g) was purified by HPLC (multiple injections) on a Vydac C-18 column (10 μ, 2.2 x 25 cm) eluting with 30% acetonitrile in 0.1% aqueous TFA over 90 minutes at a flow rate of 8 mL/min. Fractions were collected, analyzed by HPLC and pure fractions pooled and lyophilized to give 47 mg of pure peptide. Amino acid analysis: Ala 1.01 (1.0), Glx 2.00 (2.0), He 1.02 (1.0), Leu 1.06 (1.0), Thr 0.78 (1.0), Tyr 0.98 (1.0), Val 0.93 (1.0). FAB/MS: MH + 936 (calcd 936) . EXAMPLE 3: Preparation of Acetyl-tyrosyl-threonyl- aspartyl-leucyl-valyl-alanyl-isoleucyl- glutamine amide. The peptide was prepared on ABI model 431A peptide synthesizer using Version 1.12 of the standard scale Boc software modified for N-terminal acetylation according the instrument operations manual. 4- Methylbenzhydrylamine resin (0.625 g, 0.5 mmol) was used in the synthesis. Final weight of the peptide resin was 1.23 g. The peptide was cleaved from the resin (1.11 g) with 10 L of HF and 1 mL of anisole for 60 minutes at 0° C. The HF was removed by a nitrogen stream. The resulting solid was triturated with ether, collected by filtration and washed with ether. The peptide was extracted from the resin with 50% TFA and methylene chloride (5 20 L) . The resin was removed by filtration, the solvents removed under reduced pressure and the residue triturated with ether to give 0.50 g of crude peptide. The crude peptide was purified by preparation HPLC using a Vydac C-18 column (10 μ, 2.2 x 25 cm) eluting with a 20 to 30% gradient of acetonitrile and 0.1% aqueous TFA over 140 minutes at a flow rate of 3 mL per minute. Fractions were collected, analyzed by HPLC and pure fractions pooled and lyophilized to give 60 mg of the purified peptide as a white solid. Amino acid analysis: Tyr 0.99 (1.0), Thr 0.91 (1.0), Asx 0.98 (1.0), Leu 1.03 (1.0), Val 1.05 (1.0), Ala 1.03 (1.0), He 1.00 (1.0), GlX 0.01 (1.0) . EXAMPLE 4: Preparation of Tyrosyl-threonyl-aspartyl- leucyl-valyl-alanyl-isoleucyl-glutamine amide. The peptide was prepared by manual solid phase synthesis using Boc chemistry. The amino acids used were Boc-(BrCBZ)Tyr, Boc-(Bzl)Thr, Boc-(Bzl)Asp, Boc- Leu, Boc-Val, Boc-Ile and Boc-Gln. 4- Methylbenzhydrylamine resin (6.25 g, 5.0 mmol) was used in synthesis. 20 Mmol of each Boc-AA was activated by dicyclohexylcarbodiimide and hydroxybenzotriazole (20 mmol of each) and coupled to the resin. The sequence used was as follows: WASH REPETITIONS TIME'mins) 25% TFA/CH 2 C1 2 1 3 50% TFA/CH 2 C1 2 1 16 CH 2 C1 2 1 13 5% N-methylmorpholine/CH 2 Cl 2 1 4 CH 2 C1 2 1 3 Coupling step (monitored by ninhydrin testing of a resin sample) . The final weight of the peptide-resin was 11.97 g. The resin-peptide (11.8 g) was treated with 12 mL of anisole and 120 mL of HF for one hour at 0° to 4°C. The HF was removed by nitrogen stream followed by aspiration. The resultant solids were triturated with ether (1 x 100 mL then 1 x 80 mL) , collected by filtration and washed with ether (3 x 100 mL) . The residue was then extracted with 50% trifluoroacetic acid/methylene chloride (4 x 50 mL) , and the solvents removed by vacuum. The residue was triturated with 500 mL of diethyl ether. The solids were collected by filtration and air-dried overnight at ambient temperature followed by drying in vacuo at room temperature for 1 hour. The yield of crude peptide was 4.08 g. The crude peptide (106 mg) was purified in two 53 mg runs by reverse phase HPLC using Vydac 22 x 250 mm C-18, 10 μ 300 Angstrom pore packed column. Elution with a gradient of 25% to 40% B over 72 minutes at a flow rate of 6 mL/min was carried out (solvent A = 0.1% TFA; solvent B = 0.1% TFA in 50% acetonitrile/Water) . Fractions were collected and the appropriate fractions pooled to give 56.8 mg of wtl te solid. Amino Acid Analysis: Asx 1.02 (1.00), Thr 0.89 (1.00), Glx 0.99(1.00, Ala 1.02 (1.00), Val 0.96 (1.00), He 1.03 (1.00), Leu 1.06 (1.00), Tyr 0.91 (1.00). FAB/MS: MH + = 922 (calcd 922). EXAMPLE 5: Preparation of Arginyl-tyrosyl-threonyl- aspartyl-leucyl-valyl-alanyl-isoleucyl- glutamine amide. The peptide was prepared on a DuPont RAMPS system using the FMOC strategy. The amino acids used for the synthesis were FMOC-(Mtr)Arg, FMOC-(t-Bu)Tyr, FMOC-(t-Bu)Thr, FMOC-(t-Bu)Asp, FMOC-Leu, FMOC-Val, FMOC-Ala, FMOC-He and FMOC-Gln. DuPont rapid amide resin (0.1 mmol) was used in the synthesis. The peptide was cleaved from the resin using a mixture of phenol (0.25 g) , ethanedithiol (0.083 mL) , thioanisole (0.66 mL) , water (0.166 mL) and trifluoroacetic acid (3.33 mL) for 6 hours for 20° C. The resin was removed by filtration and the peptide precipitated from the filtrate by the addition of ether. The solids were removed by filtration, extracted with 20% acetic acid and lyophilized to give 0.147 g of crude peptide. The peptide was purified by preparative reverse phase (C-18) HPLC using an acetonitrile-water gradient in 0.1% in TFA. Fractions were collected and those containing pure peptide were pooled and lyophilized. EXAMPLE 6: Preparation of Asparaginyl-arginyl-tyrosyl- threonyl-aspartyl-leucyl-valyl-alanyl- isoleucyl-gluta ine amide. The peptide was prepared using a DuPont RAMPS system and the FMOC strategy. The amino acids used were FMOC-Asn, FMOC-(Mtr)Arg, FMOC-(t-Bu)Tyr, FMOC- (t-Bu)Thr, FMOC-(t-Bu)Asp, FMOC-Leu, FMOC-Val, FMOC- Ala, FMOC-Ile and FMOC-Gln. DuPont rapid amide resin (0.2 mmol) was used in the synthesis. The peptide was cleaved in the resin using a mixture of TFA (2.85 mL) , thioanisole (0.135 mL) and ethanedithiol (0.015 mL) for 16 hours at ambient temperature. The resin was removed by filtration and the peptide precipitated from the filtrate by the addition of ether. The peptide was removed by filtration, extracted with 20% acetic acid and lyophilized to give 50 mg of crude peptide. The crude peptide was purified by preparative reverse phase (C-18) HPLC using a gradient of acetonitrile water in 0.1% TFA. Fractions were collected and those containing the pure peptide were pooled and lyophilized. EXAMPLE 7: Preparation of Cysteinyl-glutaminyl- asparaginyl-arginyl-tyrosyl-threonyl- aspartyl-leucyl-valyl-alanyl-isoleucyl- glutaminyl-asparaginyl-lysyl-asparaginyl- glutamine. The peptide was prepared on an ABI model 430A peptides synthesizer using the standard scale Boc software. The amino acids used were Boc-(4-Me- Bzl)Cys, Boc-Gln, Boc-Asn, Boc-(Tos)Arg, Boc- (BrCBZ)Tyr, Boc-(Bzl)Thr, Boc-(Bzl)Asp, Boc-Leu, Boc- Val, Boc-Ala, Boc-Ile, Boc-(Cl-CBz)Lys. Boc-(Bzl)Glu- Pam resin (0.5 mmol) was used in the synthesis. The peptide was cleaved from the resin using 10 mL of HF, 1.0 mL of anisole, l.o mL of dimethyl sulfide and 0.2 mL p-thiocresol for 30 minutes at -10° C followed by 30 minutes at 0°C. The hydrogen fluoride was removed under reduced pressure and the residue triturated with ether. Solids were removed by filtration and the peptide extracted from the resin using 20% acetic acid. Removal of the resin by filtration and lyophilization of the filtrate gave 25 mg of crude peptide. The crude peptide was purified by the preparative HPLC using a 2.2 x 25 cm Synchrom C-18 column (6.5 μ) , eluting with a gradient of 5 to 25% acetonitrile in 0.1% TFA over 20 minutes at a flow rate of 6 mL per minute. Fractions were collected and the fractions containing the pure peptide and pooled lyophilized. EXAMPLE 8: Preparation of Tyrosyl-threonyl-D-aspartyl- leucyl-valyl-alanyl-isoleucyl-glutamine amide. The peptide was prepared on an ABI Model 431A peptide synthesizer using Version 1.12 of the standard Boc software. The amino acids used were Boc- (BrCBZ)Tyr, Boc-(Bzl)Thr, Boc-D-(Bzl)Asp, Boc-Leu, Boc-Val, Boc-Ala, Boc-Ile and Boc-Gln. 4- Methylbenzhydrylamine resin (0.63 g, 0.5 mmol) was used in the synthesis. The final weight of the peptide resin was 1.43 g. The peptide was cleaved from the resin (1.43 g) using 15 L of HF and 1.5 mL of anisole for 60 min at 0°C. The hydrogen fluoride was removed under reduced pressure and the residue triturated with ether. Solids were removed by filtration and the peptide extracted from the resin using a 50% solution of trifluoroacetic acid in methylene chloride. Removal of the resin by filtration and precipitation with ether gave 1.09 g of crude peptide. The crude peptide (0.5 g) was purified by preparative HPLC using a Vydac C-18 column (15 μ, 5.0 x 25 cm) eluting with a 0-100% gradient of 50% acetonitrile in 0.1% TFA over 120 minutes at a flow rate of 15 mL per minute. Fractions were collected, analyzed by HPLC and pure fractions pooled and lyophilized to give 200 mg of the desired product. Amino acid analysis: Ala 0.99 (1.00), Asx 1.01 (1.00), Glx 1.02 (1.00), He 0.97 (1.00), Leu 1.02 (1.00), Thr 0.91 (1.00), Tyr 0.96 (1.00), Val 1.04 (1.00). FAB/MS: MH + = 921 EXAMPLE 9: Preparation of Phenylalanyl-threonyl- aspartyl-leucyl-valyl-alanyl-isoleucyl- glutamine amide. The peptide was prepared on an ABI Model 431A peptide synthesizer using Version 1.12 of the standard Boc software. The amino acids used were Boc-Phe, Boc- (Bzl)Thr, Boc-(Bzl)Asp, Boc-Leu, Boc-Val, Boc-Ala, Boc-Ile and Boc-Gln. 4-Methylbenzhydrylamine resin (0.625 g, 0.5 mmol) was used in the synthesis. The final weight of the resin was 1.18 g. The peptide was cleaved from the resin (1.10 g) using 11 mL of HF and 1.1 mL of anisole for 60 min at 0°C. The hydrogen fluoride was evaporated using a stream of nitrogen and the resulting mixture triturated with ether. Solids were removed by filtration and extracted with 25 mL of a 50% solution of trifluoroacetic acid in methylene chloride. Removal of the resin by filtration, evaporation of the solvent and trituration of the residue with ether gave 0.52 g of crude peptide. The crude peptide (82 mg) was purified on a Vydac C-18 column (10 μ, 2.2 x 25 cm) eluting with a 0-60% gradient of acetonitrile and 1% TFA over 60 minutes at a flow rate of 8 mL per minute. Fractions were collected, analyzed by HPLC and pure fractions pooled and lyophilized to give 27 mg. Amino acid analysis: Ala 1.01, (1.0), Asx 1.02 (1.0), Glx 1.00 (1.0), He 0.96 (1.0), Leu 1.01 (1.0), Phe 0.94 (1.0), Thr 0.85 (1.0), Val 1.02 (1.0). FAB/MS: MH + 906. EXAMPLE 10: Preparation of D-Tyrosyl-threonyl- aspartyl-leucyl-valyl-alanyl- isoleucyl-glutamine amide. The peptide was prepared on a ABI Model 431A peptide synthesizer using Version 1.12 of the standard scale Boc software. The amino acids used were Boc-D- (BrCBZ)Tyr, Boc-(Bzl)Thr, Boc-(Bzl)Asp, Boc-Leu, Boc- Val, Boc-Ala, Boc-Ile, Boc-Gln. 4- Methylbenzhydrylamine resin (0.665 g, 0.5 mmol) was used in the synthesis. The final weight of the resin was 2.10 g. The peptide was cleaved from the resin (2.10 g) using 20 mL of hydrogen fluoride and 2 mL of anisole for 60 minutes at 0°C. The hydrogen fluoride was evaporated using a stream of nitrogen and the resulting mixture triturated with ether. The solids were removed by filtration and extracted with a 50% solution of trifluoroacetic acid in methylene chloride. Removal of the resin by filtration, evaporation of the solvent and trituration of the residue with ether gave 1.96 g of crude peptide containing residual solvents. The crude peptide (200 mL) was purified on a Vydac C-18 column (10 μ, 2.2 x 25 cm) eluting with a 0-100% gradient of 50% acetonitrile and 0.1% TFA over 120 minutes at a flow rate of 15 mL per minute. Fractions were collected, analyzed by HPLC and pure fractures pooled and lyophilized to give 52 mg of pure product. Amino acid analysis: Ala 0.99 (1.0), Asx 1.04 (1.0), Glx 1.00 (1.0), He 0.96 (1.0), Leu 0.99 (1.0), Thr 0.92 (1.0), Tyr 0.99 (1.0), Val 1.04 (1.0). FAB/MS: MH + 921. EXAMPLE 11: Preparation of Tyrosyl-D-threonyl- aspartyl-leucyl-valyl-alanyl- isoleucyl-gluta ine amide. The peptide was prepared on an ABI Model 431A peptide synthesizer using Version 1.12 of the standard Boc software. The amino acids used were: Boc- (BrCBZ)Tyr, Boc-D-(Bzl)Thr, Boc-(Bzl)Asp, Boc-Leu, Boc-Val, Boc-Ala, Boc-Ile and Boc-Gln. 4- Methylbenzhydrylamine resin (0.685 g, 0.5 mmol) was used in the synthesis. The final weight of the peptide resin was 1.63 g. The peptide was cleaved from the resin (1.63 g) using 20 mL of hydrogen fluoride and 2 mL of anisole for 60 min at 0°C. The hydrogen fluoride was removed under reduced pressure and the residue triturated with ether. The solids were removed by filtration and the peptide extracted from the resin with a 50% solution of trifluoroacetic acid in methylene chloride. Removal of the resin by filtration and precipitation with ether gave 0.52 g of crude peptide. The crude peptide (0.50 g) was purified on a Vydac C-18 column (15 μ, 5.0 x 25 cm) in four injections, eluting with a 0-100% gradient of 50% acetonitrile in 0.1% TFA over 120 minutes at a flow rate of 15 mL per minute. Fractions were collected, analyzed by HPLC and pure fractions pooled and lyophilized to give 254 mg of pure peptide. Amino acid analysis: Ala 1.01 (1.0), Asx 1.08 (1.0), Glx 0.98 (1.0), He 0.98 (1.0), Leu 0.97 (1.0), Thr 0.95 (1.0), Tyr 0.98 (1.0), Val 1.01 (1.0). FAB/MS: MH + 922. EXAMPLE 12: Inhibition of Neutrophil Binding to GMP140 Coated Wells. Binding of various peptides to GMP-140 coated wells, as described above, were compared. The results are shown in Figure 1. Binding of the peptides at various concentrations, ranging from 0 to 1.5 mM, were compared. The peptides tested were Cys-Gln-Asn-Arg- Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-amide; Asn-Arg-Tyr- Thr-Asp-Leu-Val-Ala-Ile-Gln-amide; Arg-Tyr-Thr-Asp- Leu-Val-Ala-He-Gln-amide; Tyr-Thr-Asp-Leu-Val-Ala- He-Gln-amide; Acetyl-Tyr-Thr-Asp-Leu-Val-Ala-He- Gln-amide; Tyr-Thr-Glu-Leu-Val-Ala-He-Gln-amide; Tyr- Thr-His-Leu-Val-Ala-He-Gln-amide; Tyr-Thr-Asp-Leu- Val-Ala-He-Gln-Asn-Lys-Asn-Glu-amide; Leu-Gln-Thr- Ala-Tyr-Asp-Val-He-amide (negative control) . In subsequent studies, additional peptides were tested for activity in inhibiting neutrophil addition to immobilized P-selectin. The IC 50 data is presented in mM concentration. The results are shown below in Table 1. TABLE l: INHIBITION OF BINDING OF NEUTROPHILS BY PEPTIDES STRUCTURE IC 50 (mM) CRGDLVAIQ-NH 2 .132 QNRYTDLVAIQ-NH 2 .034 NRYTDLVAIQ-NH 2 .039 NRYTDLVAIQNKNE-NH 2 -615 CYTDLVAIQ-NH 2 -364 YTDLVAIQ-NH, .262 Formyl-YTDLVAIQ-NH 2 •931 4-Br-Phe-TDLVAIQ-NH 2 .090 4-NH 2 -Phe-TDLVAIQ-NH 2 .383 Ac-RGDLVAIQ-NH 2 .179 YTALVAIQ-NH 2 .184 YTDAVAIQ-NH 2 .347 RGHLVAIQ-NH 2 .033 RGDLVAIQ-NH 2 .041 RTDLVAIQ-NH 2 .622 YTNLVAIQ-NH 2 .271 YTDLVAIN-NH 2 .187 CGDLVAIQ-NH 2 .304 YTDLVaIQ-NH 2 -420 YTdLVAIQ-NH 2 .385 YTDLVAIq-NH 2 .146 YTDLVAiQ-NH 2 •162 YTD1VAIQ-NH 2 .869 YtDLVAIQ-NH 2 .271 yTdLVAIQ-NH 2 .216 yTDLVAIQ-NH 2 .316 YTDLVIQ-NH 2 .463 YTDVAIQ-NH 2 .296 desamino-Arg-TDLVAIQ-NH 2 .707 desamino-Tyr-TDVAIQ-NH 2 . 16 YTDLVAI-descarboxy-Gln-NH 2 .391 YTQLVAIQ-NH 2 -097 TABLE 1 CONTINUED STRUCTURE YTDLVAIQ-NH-n-Bu ETDLVAIQ-NH 2 YEDLVAIQ-NH 2 YTELVAIQ-NH 2 YTDEVAIQ-NH 2 YGDLVAIQ-NH 2 YTHLVAIQ-NH 2 KTDLVAIQ-NH 2 YKDLVAIQ-NH 2 YTKLVAIQ-NH 2 N-Me-Tyr-TDLVAIQ-NH 2 Nal-TDLVAIQ-NH 2 0-Me-Tyr-TDLVAIQ-NH 2 FTDLVAIQ-NH 2 YTFLVAIQ-NH 2 Pya-TDLVAIQ-NH 2 YSDLVAIQ-NH 2 YTDLTAIQ-NH 2 Tic-TDLVAIQ-NH 2 YTDVAAIQ-NH 2 YTGLVAIQ-NH 2 Ac-YtHLVAIq-NH-n-Bu Ac-YtDLVAIQ-NH-n-Bu YTDLVAIQN-NH 2 YTDLVAIQNK-NH 2 Abbreviations: Nal - Naphthylalanine O-Me-Tyr - O-methyltyrosine N-Me-Tyr - Nα-methyltyrosine Pya - Pyridylalanine n-Bu - n-butyl Tic - tetrahydroisoquinoline carboxylic acid The results demonstrate that, with the exception of the negative control, the peptides all inhibit neutrophil binding to immobilized GMP-140. EXAMPLE 13: Modification of peptide stability in serum. Figure 2 shows the significant increase in stability against enzymes found in human serum that can be achieved by the modifications set down in Formula I and II, graphing percent of peptide remaining versus time, for two peptides: Ac-Y-T-D-L-V-A-I-Q-NH 2 and Y-T-D-L-V-A-I-Q-NH 2 . The half-life in serum increased from 20 minutes for the unmodified peptide to four hours, 37 minutes for the modified peptide. Modifications and variations of the present invention, synthetic peptides and methods for modulating binding reactions involving selectins, will be obvious to those skilled in the art from the foregoing detailed description. Such modifications and variations are intended to come within the scope of the appended claims. SEQUENCE LISTING (1) GENERAL INFORMATION: (i) APPLICANT: Heavner, George A. McEver, Rodger P. Geng, Jian-Guo (ii) TITLE OF INVENTION: Peptide Inhibitors of Inflammation (iii) NUMBER OF SEQUENCES: 45 (iv) CORRESPONDENCE ADDRESS: (A) ADDRESSEE: Kilpatrick & Cody (B) STREET: 100 Peachtree Street (C) CITY: Atlanta (D) STATE: Georgia (E) COUNTRY: US (F) ZIP: 30303 (V) 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 #1.25 (vi) CURRENT APPLICATION DATA: (A) APPLICATION NUMBER: US 07/699693 (B) FILING DATE: 14-MAY-1991 (C) CLASSIFICATION: (viii) ATTORNEY/AGENT INFORMATION: (A) NAME: Pabst, Patrea L. (B) REGISTRATION NUMBER: 31,284 (C) REFERENCE/DOCKET NUMBER: OMRF-CTCIOO (ix) TELECOMMUNICATION INFORMATION: (A) TELEPHONE: 404-572-6508 (B) TELEFAX: 404-658-6555 (2) INFORMATION FOR SEQ ID NO:l: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal ( i) SEQUENCE DESCRIPTION: SEQ ID NO:l: Tyr Thr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:2: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (V) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:2: Tyr Thr His Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:3: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:3 Tyr Thr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:4: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:4: Cys Gin Asn Arg Tyr Thr Asp Leu Val Ala He Gin 1 5 10 (2) INFORMATION FOR SEQ ID NO:5: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:5: Asn Arg Tyr Thr Asp Leu Val Ala He Gin 1 5 10 (2) INFORMATION FOR SEQ ID NO:6: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal ( i) SEQUENCE DESCRIPTION: SEQ ID NO:6: Arg Tyr Thr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:7: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal ( i) SEQUENCE DESCRIPTION: SEQ ID NO:7: Tyr Thr Glu Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:8: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 12 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:8: Tyr Thr Asp Leu Val Ala He Gin Asn Lys Asn Glu 1 5 10 (2) INFORMATION FOR SEQ ID NO:9: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:9: Tyr Thr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:10: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:10: Phe Thr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:11: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:11: Tyr Thr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:12: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (V) FRAGMENT TYPE: N-terminal ( i) SEQUENCE DESCRIPTION: SEQ ID NO:12: Tyr Thr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:13: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:13: Tyr Thr Phe Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:14: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:14: Tyr Thr Lys Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:15: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:15: Lys Thr Asp Leu Val Ala He Gin 1 5 i (2) INFORMATION FOR SEQ ID NO:16: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:16: Tyr Thr Ala Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:17: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 17: Phe Thr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:18: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:18: Tyr Thr Asp Ala Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:19: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:19: Tyr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:20: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: C-terminal ( i) SEQUENCE DESCRIPTION: SEQ ID NO:20: Cys Arg Gly Asp Leu Val Ala He Gly 1 5 (2) INFORMATION FOR SEQ ID NO:21: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 11 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:21: Gin Asn Arg Tyr Thr Asp Leu Val Ala He Gin 1 5 10 (2) INFORMATION FOR SEQ ID NO:22: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE : N-terminal (Xi) SEQUENCE DESCRIPTION : SEQ ID NO : 22 : Asn Arg Tyr Thr Asp Leu Val Ala He Gin Asn Lys sn Glu 1 5 10 (2) INFORMATION FOR SEQ ID NO:23: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal ( i) SEQUENCE DESCRIPTION: SEQ ID NO:23 Cys Tyr Thr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:24: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:24: Arg Gly His Leu Val Ala He Gly 1 5 (2) INFORMATION FOR SEQ ID NO:25: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:25: Arg Gly Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:26: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal ( i) SEQUENCE DESCRIPTION: SEQ ID NO:26: Arg Thr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:27: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:27: Tyr Thr Asn Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:28: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:28: Tyr Thr Asp Leu Val Ala He Asn 1 5 (2) INFORMATION FOR SEQ ID NO:29: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:29; Cys Gly Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:30: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:30: Tyr Thr Asp Leu Val He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:31: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 7 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal ( i) SEQUENCE DESCRIPTION: SEQ ID NO:31: Tyr Thr Asp Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:32: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:32 Tyr Thr Gin Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:33: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:33 Glu Thr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:34: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:34: Tyr Glu Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:35: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:35: Tyr Thr Asp Glu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:36: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:36: Tyr Gly Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:37: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:37 Lys Thr Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:38: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:38: Tyr Lys Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:39: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:39; Tyr Thr Lys Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO: 0: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal ( i) SEQUENCE DESCRIPTION: SEQ ID NO:40: Tyr Ser Asp Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:41: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:41: Tyr Thr Asp Leu Thr Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:42: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO:42: Tyr Thr Asp Val Ala Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:43: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:43: Tyr Thr Gly Leu Val Ala He Gin 1 5 (2) INFORMATION FOR SEQ ID NO:44: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal (Xi) SEQUENCE DESCRIPTION: SEQ ID NO:44: Tyr Thr Asp Leu Val Ala He Gin Asn 1 5 (2) INFORMATION FOR SEQ ID NO:45: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iv) ANTI-SENSE: NO (v) FRAGMENT TYPE: N-terminal ( i) SEQUENCE DESCRIPTION: SEQ ID NO:45: Tyr Thr Asp Leu Val Ala He Gin Asn Lys 1 5 10

Claims: We claim: 1. A peptide derived from selectins selected from the group consisting of the structures: R 1 -X-P-Q-S-T-U-V-W-Z-Y-R 2 (I) R 1 -P-Q-S-T-U-V-W-Z-R 2 (II) or a pharmaceutically acceptable salt thereof, wherein: X in Formula (I) and P in Formula (II) are the N-terminus amino acids, and R 1 is a moiety attached to the amine function (NHR 1 ) , Y in Formula (I) and Z in Formula (II) are the C-terminus amino acids, and R 2 is the moiety attached to the singly-bonded oxygen in the carboxy function (C(O)OR 2 ), P is D- or L-tyrosine, D- or L-phenylalanine, D- or L-lysine, D- or L-glutamic acid, D- or L-arginine, D- or L-cysteine, D- or L- 0-R 3 -tyrosine, D- or L-N α - R -tyrosine, D- or L-4-amino phenylalanine, D- or L- R -phenylalanine, D- or L-pyridylalanine, D- or L- naphthylalanine, or D- or L-tetrahydroisoguinoline carboxylic acid, where R 3 is lower alkyl or aryl and R is halogen (fluorine, chlorine, bromine or iodine) , Q is D- or L-threonine, D- or L-lysine, D- or L- glutamic acid, D- or L-cysteine, or glycine, S is D- or L-aspartic acid, D- or L-histidine, D- or L-glutamic acid, D- or L-asparagine, D or L- glutamine, D- or L-alanine, D- or L-phenylalanine, D- or L-lysine, or glycine, T, U, V and W are independently D- or L-leucine, D- or L-isoleucine, D- or L-alanine, D- or L-valine, D- or L-alloisoleucine, glycine, D- or L-glutamic acid, D- or L-aspartic acid, D- or L-asparagine, D- or L-glutamine, D- or L-threonine, or desamino acid where desamino acid refers to the deletion of either residues T, U, V, or W from the peptide formulas I or II, Z is D- or L-glutamine, D- or L-glutamic acid and D- or L-asparagine, R 1 is H (signifying a free N-terminal group) , formyl, lower alkanoyl, aroyl or desamino (meaning the amino acid adjacent to the group R 1 , either X in formula I or P in formula 2 lacks the ce-amino group of the amino acid, and is replaced with H) , R 2 is H (signifying in a free C-terminal carboxylic acid), 0(lower alkyl), O(aryl), NR R where R 3 and R 4 are independently H or lower alkyl, or descarboxy (meaning the α-carboxylic acid group of the amino acid to which R 1 is adjacent in formula I or 2, Y or Z, respectively, is replaced with H) , and X and Y are linear chains of from one to ten amino acids. 2. The peptide of claim 1 having the structure R^X-P-Q-S-T-U-V-W-Z-Y-R 2 , wherein R 1 is H, X is Cys-Xxx-Xxx-Xxx, P is Tyr, T is Leu, U is Val, V is Ala, W is He, and Y is Asn- Lys-Xxx-Glu, where Xxx is any amino acid, and R is not OH. 3. The peptide of claim 1 of the structure R^X-P-Q-S-T-U-V-W-Z-Y-R 2 ; wherein the peptide is selected from the group consisting of a peptide wherein X is Cys-Gln-Asn-Arg and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein X is Gln-Asn-Arg, and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein X is pGlu-Asn-Arg and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein X is Asn-Arg, and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein X is Arg and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn; a peptide wherein S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn-Lys; a peptide wherein S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn-Lys- Asn; a peptide wherein S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn-Lys-Asn-Glu; a peptide wherein X is Cys-Gln-Asp-Arg, S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn-Lys-Asn-Glu; a peptide wherein X is Glu-Asn-Arg, P is Arg or Tyr, S is Asp, Lys, His, Asn, Gin, or Ala; and a peptide wherein X is Asn-Arg, P is Tyr or Arg, Q is Gly, and S is Asp, Lys, His, Asn, Gin, or Ala. 4. The peptide of claim 1 having the structure R 1 -P-Q-S-T-U-V-W-Z-R 2 wherein S is Asp or His. 5. The peptide of claim 1 selected from the group consisting of peptides having the formula Tyr- Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr- His-Leu-Val-Ala-He-Gln-NH 2 ; the formula Acetyl-Tyr- Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Cys-Gln-Asn-Arg-Tyr-Thr-Asp-Leu-Val-Ala- He-Gln-NH 2 ; the formula Asn-Arg-Tyr-Thr-Asp-Leu-Val- Ala-He-Gln-NH 2 ; the formula Arg-Tyr-Thr-Asp-Leu-Val- Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Glu-Leu-Val-Ala- He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-He- Gln-Asn-Lys-Asn-Glu-NH 2 the formula D-Tyr-Thr-Asp- Leu-Val-Ala-He-Gln-NH ",2 the formula Tyr-D-Thr-Asp- Leu-Val-Ala-Ile-Gln-NH, the formula Tyr-Thr-D-Asp- Leu-Val-Ala-He-Gln-NH, the formula Phe-Thr-Asp-Leu- Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val- Ala-D-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Ala-Val- Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Ala-Leu-Val-Ala- He-Gln-NH 2 ; the formula Tyr-Thr-Phe-Leu-Val-Ala-He- Gln-NH 2 ; the formula Tyr-Thr-Lys-Leu-Val-Ala-Ile-Gln- NH 2 ; the formula Lys-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Cys-Arg-Gly-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Gln-Asn-Arg-Tyr-Thr-Asp-Leu-Val-Ala-He- Gln-NH 2 ; the formula Asn-Arg-Tyr-Thr-Asp-Leu-Val-Ala- Ile-Gln-NH 2 ; the formula Asn-Arg-Tyr-Thr-Asp-Leu-Val- Ala-He-Gln-Asn-Lys-Asn-Glu-NH 2 ; the formula Cys-Tyr- Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Formyl- Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula 4- Br-Phe-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula 4- NH 2 -Phe-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Ac-Arg-Gly-Asp-Leu-Val-Ala-He-Gln-NH 2 ;the formula Tyr-Thr-Asp-Ala-Val-Ala-He-Gln-NH 2 ; the formula Arg- Gly-His-Leu-Val-Ala-He-Gln-NH 2 ; the formula Arg-Gly- Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Arg-Thr- Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asn- Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu- Val-Ala-Ile-Asn-NH 2 ; the formula Cys-Gly-Asp-Leu-Val- Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-D- Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala- He-D-Gln-NH 2 ; the formula Tyr-Thr-Asp-D-Leu-Val-Ala- He-Gln-NH 2 ; the formula D-Tyr-Thr-D-Asp-Leu-Val-Ala- He-Gln-NH 2 ; the formula D-Tyr-Thr-Asp-Leu-Val-Ala- He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-He-Gln- NH 2 ; the formula Tyr-Thr-Asp-Val-Ala-He-Gln-NH 2 ; the formula desamino-Arg-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula desamino-Tyr-Thr-Asp-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-He-descarboxy- Gln-NH 2 ; the formula Tyr-Thr-Gln-Leu-Val-Ala-Ile-Gln- NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH- n-Bu; the formula Glu-Thr-Asp-Leu-Val-Ala-He-Gln- NH 2 ; the formula Tyr-Glu-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Glu-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Glu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Gly-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Lys-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Lys-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Lys-Leu-Val-Ala-Ile-Gln-NH 2 ; the formula N-Me-Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Nal-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula 0-Me-Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Phe-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Phe-Leu-Val-Ala-He-Gln-NH 2 ; the formula Pya-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Ser-Asp-Leu-Val-Ala-He-Gln-NH 2 , the formula Tyr-Thr-Asp-Leu-Thr-Ala-He-Gln-NH 2 ; the formula Tic-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 , the formula Tyr-Thr-Asp-Val-Ala-Ala-He-Gln-NH 2 , the formula Tyr-Thr-Gly-Leu-Val-Ala-He-Gln-NH 2 ; the formula Ac-Tyr-D-Thr-His-Leu-Val-Ala-He-D-Gln-NH-n- Bu; the formula Ac-Tyr-D-Thr-Asp-Leu-Val-Ala-He-Gln- NH-n-Bu; the formula Tyr-Thr-Asp-Leu-Val-Ala-He-Gln- Asn-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-He-Gln- Asn-Lys-NH 2 ; and pharmaceutically acceptable acid- or base-addition salts thereof. 6. The peptide of claim 1 in combination with a pharmaceutical carrier selected from the group consisting of carriers suitable for parenteral administration, oral administration, topical administration, and controlled release formulations. 7. A method for the preparation of peptides of the structure R 1 -X-P-Q-S-T-U-V-W-Z-Y-R 2 (I) R 1 -P-Q-S-T-U-V-W-Z-R 2 (II) or a pharmaceutically acceptable salt thereof, wherein: X in Formula (I) and P in Formula (II) are the N-terminus amino acids, and R is a moiety attached to the amine function (NHR 1 ) , Y in Formula (I) and Z in Formula (II) are the C-terminus amino acids, and R 2 is the moiety attached to the singly-bonded oxygen in the carboxy function (C(O)OR 2 ), P is D- or L-tyrosine, D- or L-phenylalanine, D- or L-lysine, D- or L-glutamic acid, D- or L-arginine, D- or L-cysteine, D- or L- 0-R 3 -tyrosine, D- or L-N α - R 3 -tyrosine, D- or L-4-amino phenylalanine, D- or L- R 4 -phenylalanine, D- or L-pyridylalanine, D- or L- naphthylalanine, or D- or L-tetrahydroisoquinoline carboxylic acid, where R 3 is lower alkyl or aryl and R is halogen (fluorine, chlorine, bromine or iodine) , Q is D- or L-threonine, D- or L-lysine, D- or L- glutamic acid, D- or L-cysteine, or glycine, S is D- or L-aspartic acid, D- or L-histidine, D- or L-glutamic acid, D- or L-asparagine, D or L- glutamine, D- or L-alanine, D- or L-phenylalanine, D- or L-lysine, or glycine, ' T, U, V and W are independently D- or L-leucine, D- or L-isoleucine, D- or L-alanine, D- or L-valine, D- or L-alloisoleucine, glycine, D- or L-glutamic acid, D- or L-aspartic acid, D- or L-asparagine, D- or L-glutamine, D- or L-threonine, or desamino acid where desamino acid refers to the deletion of either residues T, U, V, or W from the peptide formulas I or II, Z is D- or L-glutamine, D- or L-glutamic acid and D- or L-asparagine, R 1 is H (signifying a free N-terminal group) , formyl, lower alkanoyl, aroyl or desamino (meaning the amino acid adjacent to the group R 1 , either X in formula I or P in formula 2 lacks the α-amino group of the amino acid, and is replaced with H) , R is H (signifying in a free C-terminal carboxylic acid) , 0(lower alkyl) , O(aryl) , NR 3 R 4 where R and R 4 are independently H or lower alkyl, or descarboxy (meaning the α-carboxylic acid group of the amino acid to which R 1 is adjacent in formula I or 2, ϊ or Z, respectively, is replaced with H) , and X and Y are linear chains of from one to ten amino acids, whereby the amino acids are added either singly or in preformed blocks of amino acids to an appropriately functionalized solid support. 8. The method of claim 7, wherein the peptide has the structure R 1 -X-P-Q-S-T-U-V-W-Z-Y-R 2 , wherein R 1 is H, X is Cys-Xxx-Xxx-Xxx, P is Tyr, T is Leu, U is Val, V is Ala, W is He, and Y is Asn- Lys-Xxx-Glu, where Xxx is any amino acid, and R 2 is not OH. 9. The peptide of claim 7 of the structure R 1 -X-P-Q-S-T-U-V-W-Z-Y-R 2 ; wherein the peptide is selected from the group consisting of a peptide wherein X is Cys-Gln-Asn-Arg and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein X is Gln-Asn-Arg, and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein X is pGlu-Asn-Arg and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein X is Asn-Arg, and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein X is Arg and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn; a peptide wherein S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn-Lys; a peptide wherein S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn-Lys- Asn; a peptide wherein S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn-Lys-Asn-Glu; a peptide wherein X is Cys-Gln-Asp-Arg, S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn-Lys-Asn-Glu; a peptide wherein X is Glu-Asn-Arg, P is Arg or Tyr, S is Asp, Lys, His, Asn, Gin, or Ala; and a peptide wherein X is Asn-Arg, P is Tyr or Arg, Q is Gly, and S is Asp, Lys, His, Asn, Gin, or Ala. 10. The method of claim 7 wherein the peptide has the structure R^P-Q-S-T-U-V-W-Z-R 2 wherein S is Asp or His. 11. The method of claim 7 wherein the peptide is selected from the group consisting of peptides having the formula Tyr-Thr-Asp-Leu-Val-Ala-He-Gln- NH 2 ; the formula Tyr-Thr-His-Leu-Val-Ala-He-Gln-NH 2 ; the formula Acetyl-Tyr-Thr-Asp-Leu-Val-Ala-He-Gln- NH 2 ; the formula Cys-Gln-Asn-Arg-Tyr-Thr-Asp-Leu-Val-Ala- Ile-Gln-NH 2 ; the formula Asn-Arg-Tyr-Thr-Asp-Leu-Val- Ala-He-Gln-NH 2 ; the formula Arg-Tyr-Thr-Asp-Leu-Val- Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Glu-Leu-Val-Ala- He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-He- Gln-Asn-Lys-Asn-Glu-NH 2 ; the formula D-Tyr-Thr-Asp- Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-D-Thr-Asp- Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-D-Asp- Leu-Val-Ala-He-Gln-NH 2 ; the formula Phe-Thr-Asp-Leu- Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val- Ala-D-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Ala-Val- Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Ala-Leu-Val-Ala- He-Gln-NH 2 ; the formula Tyr-Thr-Phe-Leu-Val-Ala-He- Gln-NH 2 ; the formula Tyr-Thr-Lys-Leu-Val-Ala-He-Gln- NH 2 ; the formula Lys-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Cys-Arg-Gly-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Gln-Asn-Arg-Tyr-Thr-Asp-Leu-Val-Ala-He- Gln-NH 2 ; the formula Asn-Arg-Tyr-Thr-Asp-Leu-Val-Ala- Ile-Gln-NH 2 ; the formula Asn-Arg-Tyr-Thr-Asp-Leu-Val- Ala-He-Gln-Asn-Lys-Asn-Glu-NH 2 ; the formula Cys-Tyr- Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Formyl- Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula 4- Br-Phe-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula 4- NH 2 -Phe-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Ac-Arg-Gly-Asp-Leu-Val-Ala-He-Gln-NH 2 ;the formula Tyr-Thr-Asp-Ala-Val-Ala-He-Gln-NH 2 ; the formula Arg- Gly-His-Leu-Val-Ala-He-Gln-NH 2 ; the formula Arg-Gly- Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Arg-Thr-Asp- Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asn-Leu- Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val- Ala-He-Asn-NH 2 ; the formula Cys-Gly-Asp-Leu-Val-Ala- He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-D-Ala- He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-He- D-Gln-NH 2 ; the formula Tyr-Thr-Asp-D-Leu-Val-Ala-He- Gln-NH 2 ; the formula D-Tyr-Thr-D-Asp-Leu-Val-Ala-He- Gln-NH 2 ; the formula D-Tyr-Thr-Asp-Leu-Val-Ala-He- Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ile-Gln-NH 2 ; the formula Tyr-Thr-Asp-Val-Ala-He-Gln-NH 2 ; the formula desamino-Arg-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula desamino-Tyr-Thr-Asp-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-He-descarboxy- Gln-NH 2 ; the formula Tyr-Thr-Gln-Leu-Val-Ala-He-Gln- NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-Ile-Gln-NH- n-Bu; the formula Glu-Thr-Asp-Leu-Val-Ala-Ile-Gln- NH 2 ; the formula Tyr-Glu-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Glu-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Glu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Gly-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Lys-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Lys-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Lys-Leu-Val-Ala-He-Gln-NH 2 ; the formula N-Me-Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Nal-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula 0-Me-Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Phe-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Phe-Leu-Val-Ala-He-Gln-NH 2 ; the formula Pya-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Ser-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Thr-Ala-He-Gln-NH 2 ; the formula Tic-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Val-Ala-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Gly-Leu-Val-Ala-He-Gln-NH 2 ; the formula Ac-Tyr-D-Thr-His-Leu-Val-Ala-He-D-Gln-NH-n- Bu; the formula Ac-Tyr-D-Thr-Asp-Leu-Val-Ala-He-Gln- NH-n-Bu; the formula Tyr-Thr-Asp-Leu-Val-Ala-He-Gln- Asn-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-He-Gln- Asn-Lys-NH 2 ; and pharmaceutically acceptable acid- or base-addition salts thereof. 12. The method for preparation of the peptide of claim 7 whereby the amino acids are assembled either singly or in preformed blocks in solution or suspension by chemical ligation techniques. 13. The method for preparation of a peptide of claim 7 whereby the amino acids are assembled either singly or in preformed blocks in solution or suspension by enzymatic ligation techniques. 14. The method for preparation of a peptide of claim 13 whereby the peptide is produced enzymatically by inserting nucleic acid encoding the peptide into an expression vector, expressing the DNA, and translating the DNA into the peptide. 15. A method for modifying binding of a selectin comprising providing a peptide selected from the group consisting of the structures R^X-P-Q-S-T-U-V-W-Z-Y-R 2 (I) P^-P-Q-S-T-U-V-W-Z-R 2 (II) or a pharmaceutically acceptable salt thereof, wherein: X in Formula (I) and P in Formula (II) are the N-terminus amino acids, and R is a moiety attached to the amine function (NHR 1 ) , Y in Formula (I) and Z in Formula (II) are the C-terminus amino acids, and R 2 is the moiety attached to the singly-bonded oxygen in the carboxy function (C(O)OR 2 ), P is D- or L-tyrosine, D- or L-phenylalanine, D- or L-lysine, D- or L-glutamic acid, D- or L-arginine, D- or L-cysteine, D- or L- O-R 3 -tyrosine, D- or L-N α - R 3 -tyrosine, D- or L-4-amino phenylalanine, D- or L- R 4 -phenylalanine, D- or L-pyridylalanine, D- or L- naphthylalanine, or D- or L-tetrahydroisoquinoline carboxylic acid, where R 3 is lower alkyl or aryl and R4 is halogen (fluorine, chlorine, bromine or iodine) , Q is D- or L-threonine, D- or L-lysine, D- or L- glutamic acid, D- or L-cysteine, or glycine, S is D- or L-aspartic acid, D- or L-histidine, D- or L-glutamic acid, D- or L-asparagine, D or L- glutamine, D- or L-alanine, D- or L-phenylalanine, D- or L-lysine, or glycine, T, U, V and W are independently D- or L-leucine, D- or L-isoleucine, D- or L-alanine, D- or L-valine, D- or L-alloisoleucine, glycine, D- or L-glutamic acid, D- or L-aspartic acid, D- or L-asparagine, D- or L-glutamine, D- or L-threonine, or desamino acid where desamino acid refers to the deletion of either residues T, U, V, or W from the peptide formulas I or II, Z is D- or L-glutamine, D- or L-glutamic acid and D- or L-asparagine, R 1 is H (signifying a free N-terminal group) , formyl, lower alkanoyl, aroyl or desamino (meaning the amino acid adjacent to the group R 1 , either X in formula I or P in formula 2 lacks the α-amino group of the amino acid, and is replaced with H) , R 2 is H (signifying in a free C-terminal carboxylic acid), 0(lower alkyl), O(aryl) , NR 3 R 4 where R 3 and R 4 are independently H or lower alkyl, or descarboxy (meaning the α-carboxylic acid group of the amino acid to which R 1 is adjacent in formula I or 2, Y or Z, respectively, is replaced with H) , and X and Y are linear chains of from one to ten amino acids, in combination with a pharmaceutically acceptable carrier. 16. The method of claim 15 wherein the peptide is of the structure R 1 -X-P-Q-S-T-U-V-W-Z-Y-R 2 , wherein R 1 is H, X is Cys-Xxx-Xxx-Xxx, P is Tyr, T is Leu, U is Val, V is Ala, W is He, and Y is Asn- Lys-Xxx-Glu, where Xxx is any amino acid, and R 2 is not OH. 17. The method of claim 15 wherein the peptide is of the structure R 1 -X-P-Q-S-T-U-V-W-Z-Y-R 2 and is selected from the group consisting of a peptide wherein X is Cys-Gln-Asn-Arg and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein X is Gln-Asn-Arg, and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein X is pGlu-Asn-Arg and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein X is Asn-Arg, and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein X is Arg and S is Asp, Lys, His, Asn, Gin, or Ala; a peptide wherein S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn; a peptide wherein S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn-Lys; a peptide wherein S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn-Lys- Asn; a peptide wherein S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn-Lys-Asn-Glu; a peptide wherein X is Cys-Gln-Asp-Arg, S is Asp, Lys, His, Asn, Gin, or Ala and Y is Asn-Lys-Asn-Glu; a peptide wherein X is Glu-Asn-Arg, P is Arg or Tyr, S is Asp, Lys, His, Asn, Gin, or Ala; and a peptide wherein X is Asn-Arg, P is Tyr or Arg, Q is Gly, and S is Asp, Lys, His, Asn, Gin, or Ala. 18. The method of claim 15 wherein the peptide is of the structure R 1 -P-Q-S-T-U-V-W-Z-R 2 wherein S is Asp or His. 19. The method of claim 15 wherein the peptide is selected from the group consisting of peptides having the formula Tyr-Thr-Asp-Leu-Val-Ala-He-Gln- NH 2 ; the formula Tyr-Thr-His-Leu-Val-Ala-He-Gln-NH 2 ; the formula Acetyl-Tyr-Thr-Asp-Leu-Val-Ala-He-Gln- NH 2 ; the formula Cys-Gln-Asn-Arg-Tyr-Thr-Asp-Leu-Val- Ala-He-Gln-NH 2 ; the formula Asn-Arg-Tyr-Thr-Asp-Leu- Val-Ala-He-Gln-NH 2 ; the formula Arg-Tyr-Thr-Asp-Leu- Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Glu-Leu-Val- Ala-Ile-Gln-NH,; the formula Tyr-Thr-Asp-Leu-Val-Ala- He-Gln-Asn-Lys-Asn-Glu-NH 2 , the formula D-Tyr-Thr- Asp-Leu-Val-Ala-He-Gln-NH 2 , the formula Tyr-D-Thr- Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-D- Asp-Leu-Val-Ala-He-Gln-NH 2 , the formula Phe-Thr-Asp- Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu- Val-Ala-D-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Ala- Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Ala-Leu-Val- Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Phe-Leu-Val-Ala- Ile-Gln-NH 2 ; the formula Tyr-Thr-Lys-Leu-Val-Ala-He- Gln-NH 2 ; the formula Lys-Thr-Asp-Leu-Val-Ala-He-Gln- NH 2 ; the formula Cys-Arg-Gly-Asp-Leu-Val-Ala-He-Gln- NH 2 ; the formula Gln-Asn-Arg-Tyr-Thr-Asp-Leu-Val-Ala- He-Gln-NH 2 ; the formula Asn-Arg-Tyr-Thr-Asp-Leu-Val- Ala-He-Gln-NH 2 ; the formula Asn-Arg-Tyr-Thr-Asp-Leu- Val-Ala-He-Gln-Asn-Lys-Asn-Glu-NH 2 ; the formula Cys- Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Formyl-Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula 4-Br-Phe-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula 4-NH 2 -Phe-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Ac-Arg-Gly-Asp-Leu-Val-Ala-He-Gln-NH 2 ;the formula Tyr-Thr-Asp-Ala-Val-Ala-He-Gln-NH 2 , the formula Arg-Gly-His-Leu-Val-Ala-He-Gln-NH 2 , the formula Arg-Gly-Asp-Leu-Val-Ala-He-Gln-NH 2 , the formula Arg-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asn-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-He-Asn-NH 2 \ the formula Cys-Gly-Asp-Leu-Val-Ala-He-Gln-NH 2 j the formula Tyr-Thr-Asp-Leu-Val-D-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-Ile-D-Gln-NH 2 ; the formula Tyr-Thr-Asp-D-Leu-Val-Ala-He-Gln-NH 2 ; the formula D-Tyr-Thr-D-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula D-Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Val-Ala-He-Gln-NH 2 ; the formula desa ino- Arg-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula desamino-Tyr-Thr-Asp-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-He-descarboxy-Gln-NH 2 ; the formula Tyr-Thr-Gln-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH-n-Bu; the formula Glu-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Glu-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Glu-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Glu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Gly-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Lys-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Lys-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Lys-Leu-Val-Ala-He-Gln-NH 2 ; the formula N-Me-Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Nal-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula 0-Me-Tyr-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Phe-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Phe-Leu-Val-Ala-He-Gln-NH 2 ; the formula Pya-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Ser-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Leu-Thr-Ala-He-Gln-NH 2 ; the formula Tic-Thr-Asp-Leu-Val-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Asp-Val-Ala-Ala-He-Gln-NH 2 ; the formula Tyr-Thr-Gly-Leu-Val-Ala-He-Gln-NH 2 ; the formula Ac-Tyr-D-Thr-His-Leu-Val-Ala-He-D-Gln-NH-n- Bu; the formula Ac-Tyr-D-Thr-Asp-Leu-Val-Ala-He-Gln- NH-n-Bu; the formula Tyr-Thr-Asp-Leu-Val-Ala-He-Gln- Asn-NH 2 ; the formula Tyr-Thr-Asp-Leu-Val-Ala-Ile-Gln- Asn-Lys-NH 2 ; and pharmaceutically acceptable acid- or base-addition salts thereof. 20. The method of claim 15 wherein the pharmaceutical carrier is selected from the group consisting of carriers suitable for parenteral administration, oral administration, topical administration, and controlled release formulations,

Inventors: GENG JIAN-GUO, HEAVNER GEORGE A, MCEVER RODGER P, GENG, JIAN-GUO, HEAVNER, GEORGE, A., MCEVER, RODGER, P.
Applicants: CENTOCOR INC, REGENTS FOR THE UNIVERSITY OF, BOARD OF REGENTS FOR THE UNIVERSITY OF OKLAHOMA, CENTOCOR, INC.
Application year: 1992
Main classification: C07K7
IPC codes: A61K38, A61P7, A61P29, C07K7, C07K14