PEPTOMERS WITH ENHANCED IMMUNOGENICITY

Abstract: The present invention relates to synthetic peptide analogues useful as therapeutic agents, immunogens or for the diagnosis of disease. In particular, it relates to peptide multimers which maintain the conformation of the native proteins from which they are derived. Peptomers constructed from peptides derived from gp120 of the human immunodeficiency virus are exemplified.

Description: PEPTOMERS WITH ENHANCED IMMUNOGENICITY The present application is a continuation in part of pending application USSN 08/184,330, filed January 19, 1994. The entire application is incorporated herein by reference. BACKGROUND OF THE INVENTION The present invention relates to synthetic peptide analogues useful as therapeutic agents, immunogens or for the diagnosis of disease. In particular, it relates to ?rn&de multimers which maintain the conformation of the native proteins from which they are derived. There is a growing interest in the construction of conformationally constrained synthetic peptides analogues for use in a number of applications such as rational design of novel drugs, development of immunogens, and as components of diagnostic immunoassays. One approach useful in this effort is the construction of peptide multimers or peptomers. Construction of such multimers have been described in the prior art {see, e.g. , U. S. Patent No. 5,066,716, TJ. S. Patent No. 5,128,319, Hillman et al (1991), Cell. Immunol. 134: 1-13, and Borras-Cuesta et al. (1988), Eur. J. Immunol. 18:199-202). In certain circumstances, these peptide multimers have shown enhanced immunogenicity over the peptides from which they are derived. This technology is particularly useful in the development of assays useful for the diagnosis of infections by human immunodeficiency virus (HIV), the causative agent for AIDS. For instance, in diagnostic immunoassays, a synthetic antigen must be recognized by antibodies cross-reactive with the native antigen on the viral surface. Thus, synthetic analogues of sequences from the envelope proteins of HIV must maintain the conformation of epitopes of the native protein. U.S. Patent No. 5,128,319 describes the production of peptide multimers from sequences derived from gpl20. Evidence provided in the patent, however, indicates that antibodies raised against the multimers described there are not cross reactive with HIV envelope proteins. U.S. Patent Nos. 5,030,449, 5,081,226 and 5,283,323 disclose synthetic peptides derived from gpl20. Synthetic peptide analogues are also useful in the development of therapeutics and vaccines for the treatment and prevention of diseases such as AIDS. In the case of vaccines, safety concerns prevent the use of whole killed or attenuated HIV. Thus, most vaccines currently in clinical trials are subunit vaccines based on isolated envelope proteins from the virus. The disadvantage of this approach is that isolated proteins or fragments may be poorly immunogenic and may not contain correct epitopes to produce a protective immune response. To date, most reports of vaccines in clinical trials have been disappointing (Cohen (1993) Science 262:980-981). Thus, the development of synthetic analogues of sequences from proteins such as HIV envelope proteins which maintain conformational epitopes would be extremely useful in the development of diagnostic immunoassays and therapeutics. The present invention addresses these and other needs. SUMMARY OF THE INVENTION The present invention provides methods of detecting the presence of an antibody reactive with an HIV envelope protein in biological samples, such as blood samples. The methods comprise contacting the sample with a peptomer comprising a plurality of peptide monomers, each comprising a sequence from a CD4 binding region of gpl20 from HIV, usually HTV-1. The formation of peptomer-antibody complexes is then detected. The peptomer may be constructed using a number of techniques but are preferably constructed from haloacetyl-derivatized peptide monomers. The peptomers typically consist of about 2 to about 100 peptide monomers of about 6 to about 30 residues. A preferred peptide monomer is KIKQπNMWQEVGKAMYA (SEQ. ID. No. 7). The diagnostic assays of the invention are usually carried out using the peptomer is bound to a solid surface, such as the well of a microtiter plate. The peptomer-antibody complex is typically detected using a label, such as a detectable enzyme. The invention further provides compositions comprising a peptomer of the invention, preferably those constructed from the peptide monomer KIKQπNMWQEVGKAMYA (SEQ. ID. No.7) using haloacetyl chemistry. The peptomers of the invention can be used to block the binding of gpl20 from HIV to CD4. Thus, the compositions can be used to inhibit infection of T cells by HIV. Also provided are immunogenic compositions and methods for using them. The immunogenic compositions comprise an immunogenically effective amount of a peptomer of the invention along with a pharmaceutically accepte . \ carrier which preserves the secondary structure of the peptomer. The immunogenic compositions may further comprise an adjuvant, such as Ribi's adjuvant. Antibodies isolated from animals immunized according to the methods of the invention are also provided. Finally, vaccine compositions comprising an immunogenically effective amount of a peptomer of the invention are provided. Definitions The term "peptomer" as used herein refers to a polymer of peptide monomers. A peptomer can be a homopolymer in which all of the peptide monomers have the same sequence or a heteropolymer in which the peptide monomers have different sequences. The peptomers are preferably conformationally constrained so that particular epitopes on peptide monomers of the peptomer are in a conformation that approximates the conformation in the native protein from which the peptide is derived. A number of methods may be used to construct peptomers of the invention. Peptomers of the invention are preferably made using the haloacetyl chemistry described below. The term "peptide monomer" refers to a peptide unit used to construct a peptomer of the invention. The amino acid sequence of a peptide monomer can be derived from any biologically relevant protein, such as cellular receptors {e.g. , interleukin receptors and the like) protein ligands recognized by those receptors, or a protein antigen against which an immune response is desired. Typically, the peptide monomers are modified to facilitate construction of the peptomers of the invention. Preferred modifications of the peptides include addition of a haloacetyl moiety at the N- terminus and a cysteine residue at the C-terminus. Particular methods for the production of peptomers from peptide monomers are described in more detail below. A "pharmaceutically acceptable carrier which preserves the secondary structure of the peptomer" is a composition which preserves the secondary structure of the peptomer {i.e., either α-helix or β sheet) such that the secondary structure of the peptide monomers closely approximates the secondary structure of the native protein from which it is made. Typically, this will mean that the degree of α-helicity (if α- helical secondary structure is desired) of the peptomer in the pharmaceutical composition is at least about 20%, usually greater than about 30%, and in certain embodiments greater than about 50% as measured using circular dichroism spectroscopy as described in Provencher et al. , (1981) Biochem. 20:33-37. To preserve the secondary structure of the peptomers, the pharmaceutically acceptable carriers of the invention (including adjuvants) are preferably substantially aqueous solutions and do not comprise high concentrations of oils or other lipophilic compounds. Whether a particular carrier is suitable can easily be determined using the methods of Provencher et al. to measure the degree of α-helicity in the solution. Alternatively, antibodies raised against the compositions can be assayed for their ability to recognize the native protein. The term "peptide" is used interchangeably with "oligopeptide" or "polypeptide" in the present specification to designate a series of residues, typically L- amino acids, connected one to the other typically by peptide bonds between the α-amino and carbonyl groups of adjacent amino acids. The term "residue" refers to an amino acid or amino acid mimetic incorporated in an oligopeptide by an amide bond or amide bond mimetic. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 shows the amino acid sequence of gpl20 from the HTV-1 isolate MN. Figure 2 is a comparison of sequences from the CD4 binding regions of a number of HIV isolates. Figure 3 shows residues 419-436 of gpl20 from the MN isolate when placed in a conformational template referred to as a helical wheel. Figure 4 shows residues 419-436 of gpl20 from the MN isolate in a helical wheel along with residues from the ISYR isolate of HIV-2. Figure 5 shows the circular dichroism spectra of both the peptide and the ρeptomer(419-436). Figure 6 shows inhibition of CD4 binding to peptomer(419-436) by recombinant soluble gpl20. Open circles - recombinant gp 120. Closed circles - denatured recombinant gp 120. Figure 7 shows inhibition of the binding of biotinylated CD4 to peptomer(419-436) by benzylated CD4-derived peptides. Figure 8 shows inhibition of gpl20 binding to CD4 by peptomer(419-436). Figure 9 shows inhibition of the binding of biotinylated CD4 to peptomer(419-436) by recombinant soluble CD4. Figure 10 shows the circular dichroism spectra of both the monomeric peptide (419-436) in the presence (solid line) and absence (broken line) of the nonionic detergent Brij 35. DESCRIPTION OF THE PREFERRED EMBODIMENT The present invention provides synthetic analogues of desired proteins that can be used for the treatment and diagnosis of disease. The approach described below is particularly useful for the production of analogues in which conformational epitopes must be maintained. The following description focuses on peptomers of HIV envelope proteins used to detect antibodies to HIV, or as a therapeutic to interfere with the interaction of the virus and its target, human T cells. One of skill will recognize, however, that the methods described below can be used for other biologically relevant proteins, as well. Many theories relate HTV to the development of AIDS. One hypothesis holds that AIDS is an autoimmune disease that is induced by chronic exposure of an individual to the envelope glycoprotein of HIV, gpl6O and its major fragments gpl2O and gp41. Research has shown that a region of gpl60 shares amino acid sequence homology to a major protein of the immune system, MHC Class H /3-chain (Golding et al. (1988) J.Exp.Med. 67:914-923). Further work has shown sequence homologies between HIV-1 and other major components of the immune system such as antigen receptor molecules, immunoglobulins and T cell receptors (Sϋsal, et al. (1993) Vox Sang. 65:10-17). Because of these regions of shared sequence, an immune response against HTV-1 could result in an immune response against the immune system itself. Researchers have also found that cross-linking CD4 via gpl2O-IgG complexes and, at the same time, cross-linking T cell receptors, leads to apoptosis, or programmed cell death (Terai et al. (1991) J. Clin. Invest. 87:1710-1715). Apoptosis may account for the decrease in CD4-expressing cells that is observed in individuals suffering from ADDS. Thus, antibodies raised against certain regions of the gpl20 may promote, rather than inhibit the development of disease. Because of the potential of deleterious autoimmune responses, antibodies raised against gpl20 should be directed against regions of the protein that do not share homology with immune system proteins. For instance, the region of gpl20 involved in binding of HIV to its cellular receptor, CD4, should avoid these problems. The region of gpl2O apparently responsible for its high affinity binding to CD4 has been identified (Lasky et al. (1987) Cell 50:975-985). Workers have also shown some minor binding of radiolabeled pentadecapeptides derived from this region to HeLa cells expressing CD4 (Reed et al. (1991) Biochem. 30:4521-4527). The amino acid sequence of gpl20 from the MN isolate of HIV type 1 (HIV-1) is presented in Figure 1 and SEQ ID NO. 1. There, the CD4 binding region, the V3 loop region and the MHC homologous region are shown. Although much of the sequence of this protein is hypervariable, the CD4 binding region is relatively well conserved. A second HTV type (HIV-2) has also been described. It is believed to be more closely related to certain simian immunodeficiency viruses than to HTV-1. The envelope proteins of HIV-1 and HIV-2 share about 40% amino acid identity. The CD4 binding region of gpl20 from HIV-2 has been mapped. Otteken et al. (1993) Virology 194:37-43. A comparison of sequences from the CD4 binding region of isolates of HIV-1 and HTV-2 is shown in Figure 2 (SEQ ID Nos 2-13). Close examination of the sequences in Figure 2 reveals that they are composed of both hydrophobic amino acids and hydrophilic amino acids. When the sequence from the MN isolate is placed in a conformational template referred to as the helical wheel (Figure 3), the peptide separates into a side that is composed mostly of hydrophobic amino acids and another side that is mostly hydrophilic amino acids. This demonstration of amphipathicity implies that, under ideal conditions such as those found surrounding the peptide in the intact protein, this stretch of amino acids has the capability of being α-helical. In addition, the diagram shown in Figure 3 may shed light on the actual amino acids that are necessary for the peptide to bind to the CD4 receptor. The hydrophilic amino acids may be those exposed to the water interface of gpl2O and, therefore, may comprise the epitope recognized by neutralizing antibodies. Figure 4 is a helical wheel comparing the same region from the MN isolate to an HTV-2 sequence. Although the sequences show little sequence identity when compared linearly {see Figure 2), the helical wheel reveals that the hydrophobic sides of the two helices differ by only two amino acid residues. This observation is particularly relevant because the hydrophobic side of the helix is thought to bind CD4. Thus, synthetic analogues of these sequences from the CD4 binding region of gpl20 of HIV-1 or HIV-2 should block binding so long as they maintain an α-helical secondary structure. The production and use of such analogues is described below. A preferred method for obtaining a helical conformation is by construction of peptomers from desired oligopeptides, as described in detail below. The present invention also provides compositions comprising components which enhance the ability of the individual peptide monomers to form an α-helix. In particular, as shown in the Example section below, deterge. \ , in particular nonionic detergents, enhance the ability of the peptide monomers to form an α-helix. Peptide monomers prepared in this vsy show enhanced binding to CD4. Any of a number of detergents well known to one of skill in the art can be used in the compositions of the present invention. Suitable detergents include sodium laureate, sodium oleate, sodium lauryl sulfate, octaoxyethylene glycol monododecyl ether, octoxynol 9 and other detergents compatible with IV injection such as, TWEEN- 80 * , PLURONIC F-68 * , n-octyl-|8-D-glucopyranoside, and the like. Ionic detergents such as Gafac ® 560, sodium dodecyl sulfate and the like are also suitable. Construction of Peptomers of the invention The peptomers of the present invention comprise repeating polypeptides (peptide monomers). The peptomers may be homopolymers consisting of a single repeating peptide monomer or alternatively may be heteropolymers consisting of two or more different repeating peptide monomers or subunits. In general the peptomers may consist of about 2 to about 100 peptide monomers, usually about 5 to about 50, preferably about 10 to about 20. Each peptide monomer may range in length from about 6 to about 40 amino acid residues, usually about 10 to about 30, preferably about 12 to about 20. One of skill will recognize that the peptide monomers may be chemically synthesized or produced by means of recombinant genetics. Similarly, the peptomers may be produced by chemically linking peptide monomers together or alternatively the peptomer can be recombinantly expressed, although the peptomer is preferably produced by chemical linkage. Methods for recombinant expression of desired polypeptides is well known in the art. The polypeptides (either peptide monomers or peptomers) may be expressed in a variety of prokaryotic or eukaryotic cells. Prokaryotic cells such as E. coli are typically preferred. Alternatively, eukaryotic systems such as mammalian, insect or yeast cells can be used. For a general description of methods suitable for the recombinant expression of desired polypeptides see, e.g., Sambrook et al., Molecular Cloning - A Laboratory Manual, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, 1989. In a preferred embodiment the peptide monomers will be produced by chemical synthesis and then chemically polymerized to form a peptomer. Peptomers may be synthesized by a number of methods known to those of skill in the art. In general, peptomer synthesis involves synthesizing peptides (peptide monomers) that incorporate a reactive moiety that may be used to form a covalent linkage, either directly or through a linker, to another peptide monomer. Such reactive moieties may be naturally occurring, such as cysteine residues, or they may be non-natural, such as haloacetyl derivatized amino acids. Linkers suitable for joining peptides are well known to those of skill in the art. Generally linkers are either hetero- or homo-bifunctional molecules that contain a two reactive sites that may each form a covalent bond with the respective peptide. A number of linker molecules are well known to those of skill in the art. For example, the peptide monomers may be joined by a peptide linker, by a straight or branched chain carbon chain linker, or by a heterocyclic carbon. Heterobifunctional cross linking reagents such as active esters of N-ethylmaleimide have been widely used. See, for example, Lerner et al. (1981) Proc. Nat. Acad. Sci. (U.S.A.), 78: 3403-3407 and Kitagawa et al. (1976) J. Biochem. 79: 233-236. In a preferred embodiment, the peptomers are synthesized by the methods disclosed in U.S. Patent No. 5,066,716, copending and commonly assigned application USSN 07/715,650, filed January 14, 1991, and by Inman et al, (1991) Bioconjugate Chem. 2: 458-463. This method generally involves incorporating a haloacetyl group into a peptide monomer and then reacting that haloacetyl group with a free sulfhydryl group (or reactive amine) on another peptide monomer to form a covalent linkage between the monomers thereby creating a peptide polymer. The haloacetyl groups may be placed at any location within the polypeptide and react well with peptides containing sulfhydryl- bearing residues {e.g., cysteine). The peptide monomers are polymerized by reaction of the free sulfhydryl group on a residue in one peptide monomer with the haloacetyl group {e.g. , bromoacetyl or chloroacetyl) of another peptide monomer to form covalently linked polymeric peptides referred to as peptomers. When the peptomers of the invention are used as iir nunogens, they are preferably designed to avoid reactive groups such as free sulfhydryl groups or disulfide bonds in the final product. These groups car. l- ce part in disulfide exchange wit ' r sulfhydryl groups and disulfide bonds on host proteins in vivo and cause covalent linkages with host proteins. Thus, such composition -ay inadvertently lead to immune responses against the modified host proteins. To avoid these problems, sulfhydryl groups and other reactive sites on the peptomers of the inventions are preferably destroyed. This may be accomplished by a number of methods well known to those of skill in the art. For instance, free haloacetyl groups can be removed by treatment of the peptomers with mercaptoethanol, and the like. Similarly, free sulfhydryl groups can be removed by treatment with iodoacetamide. A) Synthesis of Peptide Monomers Peptide monomers nay be cheii-ically synthesized by a number of means well known to those of skill in the art. Solid phase synthesis in which the C-terminal amino acid of the sequence is attached to an insoluble support followed by sequential addition of the remaining amino acids in the sequence is the preferred method for preparing the peptide monomers of the present invention. Techniques for solid phase synthesis are described by Barany and Merrifield, Solid-Phase Peptide Synthesis; pp. 3- 284 in The Peptides: Analysis, Synthesis, Biology. Vol. 2: Special Methods in Peptide Synthesis, Part A., Merrifield, et al. J. (1963) Am. Chem. Soc. 85:2149-2156 and Gross and Meienhofer, eds. Academic press, N.Y., 1980 and Stewart et al., Solid Phase Peptide Synthesis, 2nd ed. Pierce Chem. Co., Rockford, 111. (1984). Peptide monomers from the desired protein may be modified as necessary to provide a number of desired attributes, e.g. , improved pharmacological characteristics, enhanced antigenicity, and the like. For instance, the peptides may be subject to various changes, such as substitutions, either conservative or non-conservative, where such changes might provide for certain advantages in their use. By conservative substitutions is meant replacing an amino ?rSύ residue with another which is biologically and/or chemically similar, e.g., one «ydrophobic residue for another, or one polar residue for another. The substitutions include combinations such as Gly, Ala; Val, lie, Leu, Met; Asp, Glu; Asn, Gin; Ser, Thr; Lys, Arg; and Phe, Tyr. The peptide monomers can also be modified by altering the order or composition of certain residues, it being readily appreciated that certain amino acid residues essential for biological activity, e.g., those critical to recognition by neutralizing anti-HIV antibodies may generally not be altered without an adverse effect on biological activity. The non-critical amino acids need not be limited to those naturally occurring in proteins, such as L-α-amino acids, or their D-isomers, but may include non-protein amino acids as well. If haloacetyl chemistry is used to construct peptomers, choice of peptide synthesis chemistry is generally constrained by the requirement that the haloacetyl moieties are stable to the reaction conditions and environments used in the synthesis and deprotection of the peptide monomer. In a preferred embodiment, peptide synthesis is performed on an automated peptide synthesizer using t-BOC based chemistry. Haloacetyl compounds may be incorporated into the peptide monomer at any location. Incorporation of the haloacetyl compound at the N terminus simply requires removal of the N-terminus protecting group {e.g. t-boc) and treatment with the haloacetic acid anhydride {see, U.S. Patent No 5,066,716). The completion of the reaction is determined by the absence of the free amine. The reaction rate can be monitored by the ninhydrin reaction of the resin according to the procedure of Sarin et al. (1981) Anal. Biochem. 117: 147-157. Incorporation of the haloacetyl compound at any other location requires coupling of a modified amino acid. Thus, for example, N°-tert-butoxycarbonyl-N'-(N- bromoacetyl-β-alanyl)-L-lysine (BBAL) may be used to place a bromoacetyl moiety at any position in the peptide monomer. See Robey et al. page 633-634 in 12th Am. Peptide Symp. June, (1992). Similarly, placement of a chloroacetyl moiety at any location within the peptide monomer may be accomplished using a chloroacetylated BBAL residue, USSN 07/715,650. Standard synthesis techniques are typically modified to account for the addition of the haloacetyl compound. The approach varies depending on the particular haloacetyl moiety and whether it is added internally to the peptide monomer or is placed in a terminal position. The details of synthesis of peptide monomers with terminal haloacetyl compounds may be found, for instance, in U.S. Patent Number 5,066,716. The synthesis of peptide monomers with internal haloacetyl compounds may be found in 07/715,650. The peptide can be cleaved and the protecting groups removed by either stirring the insoluble carrier or solid support in anhydrous, liquid hydrogen fluoride (HF) in the presence of anisole and dimethylsulfide at about 0°C for about 20 to 90 minutes, preferably 60 minutes or by bubbling hydrogen bromide (HBr) continuously through a 1 mg/10 ml suspension of the resin in trifluoroacetic acid (TFA) for 30 to 60 minutes at about room temperature, depending on the protecting groups selected. Following ethyl acetate extraction of the residual peptide-resin mixture, the peptide monomer is extracted with 0.1 M aqueous acetic acid, separated from the resin by filtration through a scintered glass filter and dried by lyophilization. Other deprotection methods well known to those of skill in the art may also be used. Introduction to Cleavage Techniques. Strategies in Peptide Sy hesis (Applied Biosystems, Foster City CA, 1990). In general, the haloacetylated peptides may be used for polymerization reactions without purification. However, if desired, the peptide monomers may be purified using standard techniques such as high performance liquid chromatography (HPLC) using a C 8 cclamn and a buffer system consisting of 0.1% trifluoroacetic acid/water/acetonitrile. Purification is generally performed under acetic conditions and low temperature {e.g. , 0°-4°C) to prevent reactions between the haloacetyl groups and the thiol groups in the peptide monomers. B) Polymerization of Monomers into Peptomers In general if the monomers are to be directly linked together, polymerization requires reacting the monomers with each other in the presence of an activating or condensing agent to induce the formation of a covalent linkage between the reactive sites on the monomers. In a preferred embodiment, the reactive sites will be chosen to react spontaneously without requiring an activating agent. Where the monomers are linked with a linker, polymer construction may be carried out in a sequential manner, first coupling the linker to a first monomer and then coupling a second monomer to the bound linker and repeating the process for each monomer coupling step. Alternatively, the linkers and monomers may be simultaneously coupled. Where it is desired to produce a heteropolymer with subunits in a particular order, sequential polymerization is preferred. Peptide monomers are generally capable of cyclization in addition to linear polymerization. Generally the tendency to cyclize may be controlled by regulating the concentration of peptide monomer in the reaction mixture. At high concentrations {e.g. 10 mg/ml or greater), predominantly linear peptomers will form, while at low concentrations {e.g. less than 1 mg/ml) peptomers will tend to cyclize. In a preferred embodiment polymerization of a haloacetylated peptide monomer may be accomplished by simply reacting the monomer with a cysteine-bearing monomer in a phosphate or carbonate buffer at pH 7-8. The reaction progresses spontaneously without a condensing or activating agent. Progress of the polymerization may be detected by titration of -SH groups with DTNB as described by Ellman (1959) Arch. Biochem. Biophys., 82:70-77. Alternatively polymerization may be evaluated by HPLC gel filtration or by SDS-PAGE (polyacrylamide gel electrophoresis), as described by Laemmli (1970) Nature (London) 227: 680-685 and staining with silver iodide or Coomassie brilliant blue. Q Isolation/Purification of Peptomer Where polymerization yields a pool of peptomers containing differing numbers of peptide monomers, it may be desired to isolate peptomers of a single length. This may be accomplished by a number of means of protein purification well known to those of skill in the art. These include, for example, gel electrophoresis, capillary electrophoresis, gel filtration, high performance liquid chromatography (HPLC), affinity chromatography, ion exchange chromatography, sizing chromatography or other protein purification techniques well known to those of skill in the art. See, for instance, Scopes, Protein Purification: Principles and Practice, Springer-Verlag: New York (1982) and Methods in Enzymology Vol. 182: Guide to Protein Purification. , Deutscher, ed. Academic Press, Inc. N.Y. (1990). D) Secondary Structure of Peptomers As noted above, in certain preferred embodiments the secondary structure of the peptomers will closely approximate the α-helical structure of the native protein. The sequence of the individual peptide monomers is selected so that the peptomer is amphipathic and the location of hydrophobic and hydrophilic residues favors an α-helical structure {see, e.g. , Kamtekar et al, (1993) Science 262:1680. The degree of α-helicity of a peptomer of the invention can be determined using standard techniques, such as circular dichroism spectroscopy {see, e.g. , Provencher et al , (1981) Biochem. 20:33-37). Using this technique, the peptomers of the invention usually show considerably more α-helical character than the peptides from which they are derived. Typically, the degree of α-helical character of the peptomers is at least about 20%, usually greater than about 30%, and in certain embodiments, greater than about 50%. Use of Peptomers in Immunoassays The invention also provides methods for detecting infection, monitoring the progression of disease or the efficacy of treatment by detection of conformational epitopes on antigens, e.g. , anti-gpl20 antibody levels in serum or other bodily fluids such as urine, saliva, cerebrospinal fluid, semen, and the like. For a review of the general procedures for performing assays of the invention, see Basic and Clinical Immunology 7th Edition (D. Stites and A. Terr ed.) 1991. The assays can be either competitive or noncompetitive. In competitive binding assays, the sample analytes {e.g. , target anti-gpl20 antibodies) compete with a labeled analyte (labeled anti-gpl20 antibodies) for specific binding sites on a capture agent (a peptomer comprising peptides from gpl20) bound to a solid surface. The concentration of labeled analyte bound to the capture agent is inversely proportional to the amount of free analyte present in the sample. Noncompetitive assays are typically sandwich assays, in which the sample analyte (target anti-gpl20 antibody) is bound between two analyte-specific binding reagents. One of the binding agents is used as a capture agent and is bound to a solid surface. The other binding agent is labelled and is used to measure or detect the resultant complex by visual or instrument means. A number of combinations of capture agent and labelled binding agent can be used. For instance, a peptomer comprising gpl20 peptides can be used as the capture agent and labelled anti-human antibodies specific for the constant region of human antibodies can be used as the labelled binding agent. Goat, sheep and other non- human antibodies specific for human immunoglobulin constant regions (eg. γ or μ) are well known in the art. Alternatively, the anti-human antibodies can be the capture agent and the peptomer can be labelled. Other proteins capable of specifically binding human immunoglobulin constant regions, such as protein A or protein G may also be used as the capture agent or labelled binding agent. These proteins are normal constituents of the cell walls of streptococcal bacteria. They exhibit a strong non-immunogenic reactivity with immunoglobulin constant regions from a variety of species. See, generally Kronval, et al. (1973) J. Immunol, 111:1401-1406, and Akerstrom, et al. (1985), J. Immunol, 135:2589-2542. The non-competitive assays need not be sandwich assays. For instance, the antibodies in the sample can be bound directly to the solid surface. The presence of antibodies to the target microorganism in the sample can then be detected using labelled antigen. Other assay formats include liposome immunoassays (LI A), which use liposomes designed to bind specific molecules (e.g., antibodies) and release encapsulated reagents or markers. The released chemicals are then detected according to standard techniques (see, Monroe et al. (1986) Amer. Clin. Prod. Rev. 5:34-41). Some assay formats do not require the use of labelled components. For instance, agglutination assays can be used to detect the presence of the target antibodies. In this case, peptomer-coated particles are agglutinated by samples comprising the target antibodies. In this format, none of the components need be labelled and the presence of the target antibody is detected by simple visual inspection. As mentioned above, depending upon the assay, various components, including the peptomer, target antibody, or anti-human antibody, may be bound to a solid surface. Many methods for immobilizing biomolecules to a variety of solid surfaces are known in the art. For instance, the solid surface may be a membrane (e.g., nitrocellulose), a microtiter dish (e.g., PVC or polystyrene) or a bead. The desired component may be covalently bound or noncovalently attached through nonspecific bonding. A wide variety of organic and inorganic polymers, both natural and synthetic may be employed as the material for the solid surface. Illustrative polymers include polyethylene, polypropylene, poly(4-methylbutene), polystyrene, polymethacrylate, poly(ethylene terephthalate), rayon, nylon, poly(vinyl butyrate), polyvinylidene difluoride (PVDF), silicones, polyformaldehyde, cellulose, cellulose acetate, nitrocellulose, and the like. Other materials which may be employed, include paper, glasses, ceramics, metals, metalloids, semiconductive materials, cements or the like. In addition, are included substances that form gels, such as proteins (e.g., gelatins), lipopolysaccharides, silicates, agarose and polyacrylamides can be used. Polymers which form several aqueous phases, such as dextrans, polyalkylene glycols or surfactants, such as phospholipids, long chain (12-24 carbon atoms) alkyl ammonium salts and the like are also suitable. Where the solid surface is porous, various pore sizes may be employed depending upon the nature of the system. In preparing the surface, a plurality of different materials may be employed, particularly as laminates, to obtain various properties. For example, protein coatings, such as gelatin can be used to avoid non-specific binding, simplify covalent conjugation, enhance signal detection or the like. If covalent bonding between a component of the assay and the surface is desired, the surface will usually be polyfunctional or be capable of being polyfunctionalized. Functional groups which may be present on the surface and used for linking can include carboxylic acids, aldehydes, amino groups, cyano groups, ethylenic groups, hydroxyl groups, mercapto groups and the like. The manner of linking a wide variety of compounds to various surfaces is well known and is amply illustrated in the literature. See for example Immobilized Enzymes, Ichiro Chibata, Halsted Press, New York, 1978, and Cuatrecasas (1970), J. Biol Chem. 245:3059. In addition to covalent bonding, various methods for noncovalently binding an assay component can be used. Noncovalent binding is typically nonspecific absorption of a compound to the surface. Typically, the surface is blocked with a second compound to prevent nonspecific binding of labelled assay components. Alternatively, the surface is designed such that it nonspecifically binds one component but does not significantly bind another. For example, a surface bearing a lectin such as Concanavalin A will bind a carbohydrate containing compound but not a labelled protein that lacks glycosylation. Various solid surfaces for use in noncovalent attachment of assay components are reviewed in U.S. Patent Nos. 4,447,576 and 4,254,082. Many assay formats employ labelled assay components. The labelling systems of the invention can be in a variety of forms. The label may be coupled directly or indirectly to the desired component of the assay according to methods well known in the art. A wide variety of labels may be used. The component may be labelled by any one of several methods. The most common method of detection is the use of autoradiography with 3 H, 125 1, 35 S, 14 C, or 32 P labelled compounds or the like. Non- radioactive labels include ligands which bind to labelled antibodies, fluorophores, chemiluminescent agents, enzymes, and antibodies which can serve as specific binding pair members for a labelled ligand. The choice of label depends on sensitivity required, ease of conjugation with the compound, stability requirements, and available instrumentation. Non-radioactive labels are often attached by indirect means. Generally, a ligand molecule (e.g., biotin) is covalently bound to the molecule. The ligand then binds to an anti-ligand (e.g., streptavidin) molecule which is either inherently detectable or covalently bound to a signal system, such as a detectable enzyme, a fluorescent compound, or a chemiluminescent compound. A number of ligands and anti-ligands can be used. Where a ligand has a natural anti-ligand, for example, biotin, thyroxine, and cortisol, it can be used in conjunction with the labelled, naturally occurring anti-ligands. Alternatively, any haptenic or antigenic compound can be used in combination with an antibody. The molecules can also be conjugated directly to signal generating compounds, e.g., by conjugation with an enzyme or fluorophore. Enzymes of interest as labels will primarily be hydrolases, particularly phosphatases, esterases and glycosidases, or oxidoreductases, particularly peroxidases. Fluorescent compounds include fluorescein and its derivatives, rhodamine and its derivatives, dansyl, umbelliferone, etc. Chemiluminescent compounds include luciferin, and 2,3-dihydrophthalazinediones, e.g., luminol. For a review of various labelling or signal producing systems which may be used, see, U.S. Patent No. 4,391,904. In another aspect, the present invention can be provided in a kit format for detecting anti-gpl20 antibodies. Such a kit includes peptomers specifically recognized by the target antibodies and a labelling system, including enzyme substrates and the like, suitable for detecting the immune complexes formed by the peptomers and target antibodies. The kits also include appropriate washing solutions, dilution buffers and the like for preparation and analysis of urine samples. Immunogenic and Pharmaceutical Compositions The peptomers of this invention may also be used as immunogens to produce antibodies against target proteins, such as gpl20. An amount adequate to accomplish this is defined here as an "immunogenically effective dose". For instance, the peptomers of the invention can be used to raise monoclonal or polyclonal antibodies that can be used to detect the presence of HIV. Antibodies which bind peptomers of the invention may be produced by a variety of means. The production of non-human monoclonal antibodies, e.g., murine, lagomorpha, equine, etc., is well known and may be accomplished by, for example, immunizing the animal with an immunogenic composition containing the polypeptide. Antibody-producing cells obtained from the immunized animals are immortalized and screened, or screened first for the production of antibody which inhibits binding between gpl20 and CD4 and then immortalized. For a discussion of general procedures of monoclonal antibody production see Harlow and Lane, Antibodies, A Laboratory Manual Cold Spring Harbor Publications, N.Y. (1988) and Antibodies in Cell Biology, Asai, D., ed. (Academic Press, San Diego, CA, 1993). As shown below, the immunogenic composition used to raise antibodies is preferably selected so as to preserve the secondary structure of the peptomer. Preservation of the secondary structure is thought to maintain conformational epitopes in the peptomer. As shown below, oil based, lipophilic adjuvants such as Freund's adjuvant, do not preserve the structure in a form that is recognized by antibodies that are also reactive with the native protein. Thus, preferred adjuvants are aqueous solutions such as Ribi's adjuvant, which contains three components extracted from bacteria, monophosphory ; lipid A, trehalose dimycolate and cell wall skeleton (MPL+TDM+ S) in a 2% squalene/Tween 80 emulsion. Other suitable adjuvants include alum, aluminum phosphate, aluminum hydroxide, N-a∞tyl-muramyl-L-threonyl-D-isoglutamine (thr-MDP) , N-acetyl-nor-muramyl-L-alanyl-D-isoglutamine (CGP 11637, referred to as nor-MDP), and N-a∞tylmuramyl-Lalanyl-D-isoglutaminyl-L-alanine-2-( -2'-dipalmitoyl-sn- glycero-3-hydroxyphosphoryloxy)-ethylamine (CGP 19835 A, referred to as MTP-PE). The effectiveness of an adjuva^ may be determined by measuring the amount of cross- reactive antibodies directed against the immunogenic peptomer. The compositions of the invention can also be administered prophylactically or to an individual already suffering from a disease. Thus, the invention also provides pharmaceutical compositions which are suitable for administration to humans, to treat and/or prevent disease, such as AIDS. Suitable formulations for this purpose are well known to those of skill in the art and can be found, for instance, in Remington's Pharmaceutical Sciences. Mack Publishing Company, Philadelphia, PA, 17th ed. (1985). The pharmaceutical compositions can administered to a patient in an amount sufficient to elicit a therapeutic or protective immune response against the target antigen, such as HIV envelope proteins. Alternatively, the peptomers can be used to directly block interaction of a disease organism with human cells. In the case of HIV infection, the peptomers should block interaction of the virus with CD4 on the surface of T cells and thus ameliorate symptoms of the disease. An amount adequate to accomplish this is defined as a "therapeutically effective dose." Amounts effective for this use will depend on, e.g., the peptomer composition, the manner of administration, the stage and severity of the HTV infection being treated, the weight and general state of health of the patient, and the judgment of the prescribing physician. For use as an immunogen, the peptomers are administered in doses which generally range for the initial immunization (that is for therapeutic or prophylactic administration) from about 0.01 mg to about 2.0 mg per 70 kilogram patient, more commonly from about 0.1 mg to about 1.0 mg per 70 kg of body weight. Boosting dosages are typically from about 0.1 mg to about 1.0 mg of peptomer using a boosting regimen over weeks to months depending upon the patient's response and condition. A suitable protocol would include injection at time 0, 3, 9, 24 and 52 weeks, followed by booster injections. When the peptomers of the invention are used to block interaction of gpl20 and CD4, they are preferably prepared using methods which preserve or enhance the solubility of the peptomer. For instance, if the peptomer is prepared using the haloacetyl chemistry described above, the final product is preferably not lyophilized. In the absence of a lyophilization step, the peptomers remain more soluble in aqueous solutions (typically solubility at least about lmg/ml, preferably at least about 2mg/ml) and have increased ability to block binding {see, Example 7). In contrast, immunogenic compositions usually comprise relatively insoluble formulations (typically solubility less than about 1 mg/ml) to increase immunogenicity. The peptomers of the invention can be used alone or in combination with other therapeutic agents such as subunit vaccines, in which case they may be used to enhance the immune response against desired regions of the antigen. For instance, the peptomers of the invention with increased solubility {e.g., prepared without a lyophilization step) can be used in combination with formulations that provide enhanced immunogenicity. Thus, such compositions can be used to directly block gpl20-CD4 binding as well as illicit an anti-gpl20 immune response. In other embodiments, a peptomer derived from the CD4 binding region of gpl20 can be used in combination with a gpl20 or gpl60 vaccine, to ensure that antibodies to the CD4 binding region are produced. Alternatively, the peptomer can be used in a boosting regimen to boost the immune response against this region. It must be kept in mind that the pharmaceutical compositions of the present invention may be employed in serious disease states, that is, life-threatening or potentially life threatening situations. In such cases, in view of the minimization of extraneous substances and the relative nontoxic nature of the peptomers of the invention, it is possible and may be felt desirable by the treating physician to administer substantial excesses of these compositions. For therapeutic use, administration should begin at the first sign of HIV infection. This is followed by boosting doses until viral load is substantially reduced or eliminated and for a period thereafter. In some circumstances, loading doses followed by boosting doses may be required. Vaccine compositions containing the peptides are administered prophylactically to a patient at risk of HIV infection to elicit an immune response against the virus. The pharmaceutical compositions are intended for parenteral or oral administration. Preferably, the pharmaceutical compositions are administered parenterally, e.g., subcutaneously, intradermally, or intramuscularly. Thus, the invention provides compositions for parenteral administration which comprise a solution of the peptomers dissolved or suspended in an acceptable carrier, preferably an aqueous carrier. A variety of aqueous carriers may be used, e.g., water, buffered water, 0.4% saline, 0.3% glycine, hyaluronic acid and the like. These compositions may be sterilized by conventional, well known sterilization techniques, or may be sterile filtered. The resulting aqueous solutions may be packaged for use as is, or lyophilized, the lyophilized preparation being combined with a sterile solution prior to administration. The compositions may contain pharmaceutically acceptable auxiliary substances as required to approximate physiological conditions, such as buffering agents, tonicity adjusting agents, wetting agents and the like, for example, sodium acetate, sodium lactate, sodium chloride, potassium chloride, calcium chloride, and the like. When peptomers of the invention are used to block CD4 binding, they are preferably used in compositions useful in preventing an initial viral infection at the point of entry into the body. Since HIV is sexually transmitted, the peptomers are conveniently included in compositions applied in the urogenital tract. For instance, such peptomers can be used with condoms or spermicidal gels. For solid compositions, conventional nontoxic solid carriers may be used which include, for example, pharmaceutical grades of alumina, mannitol, lactose, starch, magnesium stearate, sodium saccharin, talcum, cellulose, glucose, sucrose, magnesium carbonate, and the like. For oral administration, a pharmaceutically acceptable nontoxic composition is formed by incorporating any of the normally employed excipients, such as those carriers previously listed, and generally 10-95% of active ingredient, that is, one or more peptomers of the invention, and more preferably at a concentration of 25%-75%. As noted above, in some embodiments, the compositions are intended to induce an immune response against the peptomers. Thus, compositions and methods of administration suitable for maximizing the immune response are preferred. Useful carriers are well known in the art, and include, e.g., thyroglobulin, albumins such as human serum albumin, tetanus toxoid, polyamino acids such as poly(lysine:glutamic acid), influenza, hepatitis B virus core protein, hepatitis B virus recombinant vaccine and the like. In addition, adjuvants, as described above, may also be included. The concentration of peptomers of the invention in the pharmaceutical formulations can vary widely, i.e. from less than about 0.1%, usually at or at least about 2% to as much as 20% to 50% or more by weight, and will be selected primarily by fluid volumes, viscosities, etc., in accordance with the particular mode of administration selected. The following examples are provided to illustrate, but not to limit the present invention. EXAMPLE 1 Synthesis of Specific Peptomer a) Synthesis of the (419-436) peptide monomer The N-bromoacetyl peptide sequence, N- KD QIINMWQEVGKAMYA -C corresponding to residues 419 to 436 of the HIV-1 glycoprotein (gpl20), was synthesized using an automated solid phase peptide synthesizer (Model 430A, Applied Biosystems, Foster City, California, U.S.A.). As a last step in synthesis, bromoacetic acid was reacted with the amino terminal amino acid to form the N-bromoacetyl-derivatized fully protected peptide (peptide monomer). This was carried out simply by substituting 2.0 mmol of bromoacetic acid for glycine in an empty glycine cartridge as the last step in the synthesis and using the programmed run file of the automated synthesizer for the glycine coupling. Bromoacetic acid anhydride (1.0 mmol) is formed as an intermediate in the coupling reaction done on a 0.5 mmol scale. Deprotection and release of the bromoacetylated peptide from the PAM resin was accomplished by treating the resin with anhydrous hydrofluoric acid containing 10% anisole at 0°C for 2 hours. Following ethyl acetate extraction of the residual peptide-resin mixture, the peptide was extracted with 0.1 M aqueous acetic acid, separated from the resin by filtration through a scintered glass filter, and dried by lyophilization. The crude peptide was obtained in a yield of approximately 95%. If necessary the peptides can be further purified prior to polymerization using standard techniques, such as HPLC. b) Polymerization of the peptide monomers to form peptomer (419-436) The peptide polymers were prepared by dissolving 5 mg of the N- bromoacetyl cysteine-containing peptides in 1.0 ml of deoxygenated 0.5 M NaHCO 3 or 0.1 M NaHPO 4 , pH 7.0 - 7.5 buffer and stirring these solutions under N 2 for 5-12 hours at 25 °C. The resulting peptomers are generally only partially soluble water and not soluble in buffered saline solutions. They are soluble in 10% acetic acid at less than about lmg/ml. EXAMPLE 2 Immune Response of Peptomer (419-436) in Rabbits Rabbits were initially immunized with peptomer (419-436) in Freund's Complete Adjuvant followed by a single boost with Freund's Incomplete Adjuvant. In only 2 or 3 weeks there was a titer of 1:10,0000 for the antibody binding to the peptomer. However, the antibody was not able to recognize gpl2O or to neutralize HTV-1 infection in vitro. While the reasons for this are not entirely understood, it is suspected that since Freund's adjuvants are composed mostly of mineral oil the peptide is unable to retain its native conformation. Freund's adjuvants are extremely non-polar. Therefore a peptide that depends on hydrophobic interactions to maintain its conformation may change its conformation in Freund's, thereby losing its activity. Rabbits were then immunized with 1 mg of peptomer(419-436) in Ribi's adjuvant and the response is shown in Table 1. After 9 weeks, the titer against the peptomer was approximately 1:3,200. HIV-1 MN isolate was neutralized at a dilution of 1:70. Neutralization assays were carried as described in Robert-Guroff, et al. in Techniques in HIV Research Aldovini and Walker eds. pp. 179-185 (Aldrich 1990). The antibodies also reacted well with recombinant soluble gpl20 in a dot blot assay. The dot blot assays were carried as follows. Peptomers in H 2 O were spotted onto nitrocellulose paper. The nitrocellulose was then blocked with 3% bovine serum albumin in tris-buffered saline (TBS) pH 7.4 for 1 hour, then treated with 1 μg/ml biotinylated rsCD4 (Genentech, South San Francisco, CA) for 3 hours in a buffer containing TBS and 0.1 % Tween 20. The nitrocellulose was then treated with a 1:750 dilution of streptavidin-horseradish peroxidase conjugate and developed. Together these results strongly suggest that the antibodies bind to gpl2O and prevent HIV-1 from binding and infecting CD4-bearing cells. Table 1. Immune Response of Rabbits to Peptomer(419-436). Adjuvant 3 Week 9 Week gpl20 Titer Titer Reactivity Neutralization Freund's 1:10,000 1:20,000 0 None Ribi's 1:3,200 1:6,400 + + 1: 15 to 1:70 gpl2O Reactivity was in the dot blot assay. Neutralization was with an in vitro neutralization assay using the MN isolate of HIV-1. EXAMPLE 3 Immune Response of Peptomer (419-436) in Rhesus Monkeys This experiment was done with Rhesus monkeys that had been primed with various attenuated poxvirus recombinant carrying HTV-I MN genes and boosted with envelope and gag proteins formulated in alum. Six monkeys were used for the studies. Two of the monkeys were immunized with peptomer(419-436) suspended in phosphate-buffered saline (PBS at pH 7.4 without adjuvant) and four were immunized with peptomer(419-436) in alum. Each animal was injected with a single 1 ml bolus containing 1 mg peptomer(419-436) in a subscapular location in order that the immunogen be administered in a lymph node-rich locus. Three weeks after the initial injection, the monkeys were injected again and the final evaluε' was performed after an additional three weeks (a total of six weeks from the initial injection). The peak neutralization titers, for all monkeys, which ranged from 40 to 650 during previous immunizations had declined to low levels prior to administration of the peptomer (Table 2). Monkey 236L who achieved the highest neutralization titers of 620, had a titer of 25 at the time of immunization with the peptomer. Three weeks following the initial administration of the peptomer(419-436) an ELISA titer against the peptomer of 1:3,200 was detected for the monkeys immunized with peptomer in alum. No titer was detected for those monkeys immunized with peptomer in PBS. The monkeys were boosted and three weeks later, the monkeys who received peptomer in alum all had a titer equal to about 1:6,400 compared to 1:1,600 for the monkeys who received peptomer in PBS. The neutralization titers of the peptomer/PBS-immunized monkeys increased from 0 to about 1:40 - 1:50. The same appeared for the alum-containing immunogen. However, one monkey in --.ύs group did not respond to any immunogen including the poxvirus/subunit cocktails administered before these studies. Table 2. Immune Response of Rhesus Monkeys to Peptomer (419-436). HΓV-I (MN) ELISA titer NEUTRALIZATION I.D. No. Adjuvant 0 weeks 6 weeks 0 weeks 6 weeks 235L PBS 0 1,600 40 236L PBS 0 3,200 25 50 242L Alum 0 6,400 40 243L Alum 0 6,400 115 244L Alum 0 6,400 65 75 245L Alum 0 3,200 The neutralization titers are given as the reciprocal of the dilution of serum that gives a 40% neutralization of HIV-1 (MN) infection in vitro. A negative value means neutralization was not observed at the lowest serum dilution tested (1:25). The MN isolate was used because this was the strain used to design the peptomer. Sera taken prior to the immunizations from monkeys that ultimately achieved the highest neutralization titers were tested for reactivity with the peptomer in an ELISA format. No reactivity was observed. Thus, all of the monkeys, prior to receiving peptomer as an immunogen, did not produce antibodies to this region of gpl2O. After immunization with the peptomer, the monkeys did show a strong response in the ELISA. Thus a new epitope appeared due to the administration of the peptomer and the resulting boost in the in vitro neutralization was not a boost to a previous-existing titer but a new class of protective antibodies induced by the peptomer as an immunogen. In summary, peptomer(419-436) is immunogenic in Rhesus monkeys previously immunized with various HTV-related immunogens including gpl6O/120. Furthermore, it appears that peptomer(419-436) is immunogenic alone and does not require an adjuvant. This may be due to the ability of the peptomer to bind to CD4 in the monkey and this may signal the immune system to respond by producing antibodies. EXAMPLE 4 Immune Response of Peptomer(419-436) in Chimpanzees Chimpanzees provide a good model system for testing the safety and efficacy of an antigenic material prior to human studies. Four chimpanzees that have never been used in any other trial are used in this study. The chimpanzees are divided into two groups with two chimpanzees in each group. Approximately 50 ml of whole blood are obtained from each chimpanzee. The blood is clarified and clotted to provide sera which is used throughout the experiment as the "pre-bleed" control. The original sera are divided into 0.1 ml aliquots which are stored at -70°C and which are used once after thawing. All evaluations are referenced to these controls. On the first day following the prebleed, each animal, under ketamine anesthesia, is injected under the scapula (shoulder blade) with a suspension consisting of 1 mg peptomer (419-436) in 1 ml adjuvant. Each group of two chimpanzees receives the peptomer, but one group receives the peptomer in alum as adjuvant and the other with Ribi's adjuvant. The chimps are allowed to rest for three weeks after which time, under ketamine anesthesia, they are bled of 20 ml and re-immunized in the exact same fashion as on the first day. At this point, the sera obtained are tested for antibodies against the peptomer, antibodies that react with gpl2O and antibodies that block HIV-1 infection in vitro. The chimpanzees are then allowed to rest for six weeks and, after this time, a 20 ml bleed is taken. The chimpanzees are then immunized again as on day 1. The sera are again tested for the presence of anti-peptomer, anti-gpl2O and neutralizing antibodies. After 21 weeks, 20 ml bleeds are obtained to test for the titers of the antibodies. At this time, depending on antibody titer, the chimpanzees are either boosted as above or and then another test bleed is taken two weeks later, or nothing is done. After a period of 6 months expires, another 20 ml test bleed is taken and the possibility of boosting the chimps again is evaluated. If necessary, the animals are boosted again. If the titers appear suitable, the chimpanzees are returned to their normal living environment with other chimpanzees and periodically observed for health and behavioral effects. When in vitro neutralization titers believed to be protective are achieved {e.g., titers of 320-640), the chimpanzees are challenged with HIV-1 or HIV-2. The challenges is initially performed with the virus homologous to that used to produce the peptomer. Unrelated and untreated chimpanzees are used as a negative control. The onset of symptoms characteristic of HTV {e.g. reduced CD*+ T cells) is then assayed in the treated and the untreated chimpanzees. EXAMPLE 5 Secondary structure of peptomer(419-436) Circular dichroism spectroscopy was used to determine the degree of α- helicity of the peptomer and the peptide from which it was derived. Figure 5 shows the circular dichroism spectra of both the peptide and the peptomer(419-436). It is clear from the two spectra that they are considerably different and analyzing the data according to the methods of Provencher et al , (1981) Biochem. 20:33-37, indicates that the peptomer contains far more α-helical character than the peptide itself. In this case, the peptide contains 8±7% helix, while the peptomer has 31 + 1%. This establishes that by polymerizing the peptide, the peptomer achieves a conformation that is not favored for the free peptide monomer. EXAMPLE 6 Peptomer(419-436) is recognized by antisera from HIV infected individuals, while the corresponding peptide is not. Standard ELISA methods were used in these experiments. Briefly, 96- ell polystyrene plates were coated with 1 μg/well of peptide or peptomer. The results are presented in Table 3. The peptide found 9/27 (33%); the peptomer found 26/27 (96%); 1/10 (10%) false positive with the peptomer. Table 3 ELISA Xiters of HΙV-l(- ) Serum Samples: Peptide 419-436 vs. Peptomer Sample No. Diaσnosis Peotide 419-436 PeDtomer 571 HIV+ 0 1:1280 GSF2 AIDS 1: 1280 1:1280 LYM03 Hodgkins 0 0 863 HIV+ 0 1:1280 GSF3 AIDS 1: 1280 1:1280 GSF1 AIDS 0 1:1280 EYE01D Uveitis 0 0 SF53 AIDS 0 1:1280 797 HIV+ 0 1:1280 770 HIV+ 0 1:640 217 HIV+ 0 1:640 156 AIDS 0 1:1280 196 HIV+ 0 1:1280 466 HIV+ 0 1:1280 555 HIV+ 0 1:1280 37 HIV+ 0 0 GS46 AIDS 0 1:1280 LYM02 LYMPHOMA 0 0 552 HIV+ 1: 1280 1:1280 EYE08C VEITIS 0 0 LYM06 LYMPHOMA 0 0 EYE06C UVEITIS 0 1:1280 GS52 AIDS 1: 640 1:1280 864 HIV+ 1: 1280 1:1280 265 HIV+ l: 1280 1:1280 656 HIV+ 1: 1280 1:1280 80 AIDS 0 1:1280 685 HIV+ 1: 1280 1:640 GS47 AIDS 0 1:320 865 HIV+ 1: 320 1:1280 KD15 Kidney Graft 0 0 589 HIV+ 0 1:1280 862 HIV+ 0 1:640 517 HIV+ 0 1:1280 740 NORMAL 0 0 LYM-1 LYMPHOMA 0 0 7H8 Kidney Graft 0 0 EXAMPLE 7 Inhibition of binding of by peptomer 419-436. The peptomer used in the experiments described in this Example was prepared without a lyophilization step. Thus, the peptide showed increased solubility in aqueous solutions and had enhanced ability to block binding between CD4 and gpl20. A. Inhibition of biotinylated CD4 binding to peptomer(419-436) by recombinant soluble gpl20. Biotinylated CD4 was made by reacting 1.0 mg recombinant soluble CD4 (Genentech) with 15 mg. Biotin succinimide (Pierce Chem. Co.) in 0.1 M sodium bicarbonate for 30 min. Following dialysis at 4°C for 2 days into phosphate- buffered saline, the biotinylated CD4 was stored at 1 mg/ml at 4°C. To measure the inhibition of CD4 binding to peptomer(419-436) the following ELISA procedure was used: 10 μg/200 μl of the peptomer in PBS were used to coat the wells of a microtitre plate for 1 hr at room temperature, lμg/well biotinylated CD4 was used. The amount of gpl20 (native and denatured) used in the assay is shown in Figure 6. The gpl20 was denatured by SDS and beta mercaptoethanol. The biotin was detected with streptavidin-alkaline phosphatase Tago, Inc. (Burlingame, CA) at a dilution of 1:1000 and developed with p-nitrophenylphosphate. B. Inhibition of the binding of biotinylated CD4 to peptomer(419-436) by benzylated CD4-derived peptides. Using the same ELISA procedure described above, the ability of benzylated CD4-derived peptides to block binding to peptomers of the invention was shown (Figure 7). The benzylated peptides are were prepared as described by Lifson, et al. AIDS Res. Hum. Retro. 7:521-527 (1991). C. Inhibition of gp!20 binding to CD4 bv peρtomer(419-436). The ELISA procedure was the same as above except that 500 ng/well of recombinant soluble gpl20 was used to coat each well instead of peptomer. Poly-scrambled peptomer is a peptomer that contains all the amino acids as in peptomer(419-436) in a scrambled order. Results are shown in Figure 8. D. Inhibition of the binding of biotinylated CD4 to peptomer(419-436) by recombinant soluble CD4. The conditions of the E1ISA are the same as in A, above. Results are shown in Figure 9. The value of the inhibition at 50% is equal to about 1 μg/ml. This is the inhibition constant and is equal to approximately 24 nM. 24 nM is in close proximity to that value reported in the literature for binding gpl20 to CD4 which ranges from 1 nM to 45 nM. These results demonstrate that the peptomers of the invention can act as Mockers of gpl20/CD4 binding and thus inhibit infection of T cells by HIV. Example 8 Peptide monomers form α-helix in the presence of detergent Using circular dichroism spectroscopy as described in Example 5, above, the degree of α-helicity of the peptide (419-436) with and without detergent was determined. Figure 10 shows the circular dichroism spectra of the peptide in phosphate buffered saline (PBS) (broken line) and in PBS with 0.03% Brij 35 (solid line). The shoulder in the solid line at 220 λ indicates the presence of an α-helix in the peptide with detergent. These results were confirmed in assays showing enhanced ability of the peptide monomer to bind CD4 in the presence of detergent. The above examples are provided to illustrate the invention but not to limit its scope. Other variants of the invention will be readily apparent to one of ordinary skill in the art and are encompassed by the appended claims. All publications, patents, and patent applications cited herein are hereby incorporated by reference. SEQUENCE LISTING (1) GENERAL INFORMATION: (i) APPLICANT: Robey, Frank A. Harris-Kelson, Tracy A. Robert-Guroff, Marjorie (ii) TITLE OF INVENTION: PEPTOMERS WITH ENHANCED IMMUNOGENICITY (iii) NUMBER OF SEQUENCES: 13 (iv) CORRESPONDENCE ADDRESS: (A) ADDRESSEE: Townsend and Townsend Khourie and Crew (B) STREET: Steuart Street Tower, One Market Plaza (C) CITY: San Francisco (D) STATE: California (E) COUNTRY: US (F) ZIP: 94105-1493 (v) COMPUTER READABLE FORM: (A) MEDIUM TYPE: Floppy disk (B) COMPUTER: IBM PC compatible (C) OPERATING SYSTEM: PC-DOS/MS-DOS (D) SOFTWARE: Patentln Release #1.0, Version #1.25 (vi) CURRENT APPLICATION DATA: (A) APPLICATION NUMBER: US (B) FILING DATE: 19-JAN-1994 (C) CLASSIFICATION: (viii) ATTORNEY/AGENT INFORMATION: (A) NAME: Bastian, Kevin L. (B) REGISTRATION NUMBER: 34,774 (C) REFERENCE/DOCKET NUMBER: 15280-190 (ix) TELECOMMUNICATION INFORMATION: (A) TELEPHONE: (415) 543-9600 (B) TELEFAX: (415) 543-5043 (2) INFORMATION FOR SEQ ID NO:l: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 856 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: Protein (B) LOCATION: 1..856 (D) OTHER INFORMATION: /note= "Amino acid sequence of gpl20 from HIV-1 isolate MN." (ix) FEATURE: (A) NAME/KEY: Region (B) LOCATION: 401..800 (D) OTHER INFORMATION: /note= "CD4 binding region" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:l: Met Arg Val Lye Gly lie Arg Arg Aβn Tyr Gin His Trp Trp Gly Trp 1 5 10 15 Gly Thr Met Leu Leu Gly Leu Leu Met lie Cys Ser Ala Thr Glu Lys 20 25 30 Leu Trp Val Thr Val Tyr Tyr Gly Val Pro Val Trp Lye Glu Ala Thr 35 40 45 Thr Thr Leu Phe Cyβ Ala Ser Aβp Ala Lye Ala Tyr Aβp Thr Glu Val 50 55 60 His Asn Trp Trp Ala Thr Gin Ala Cys Val Pro Asp Thr Pro Asn Pro 65 70 75 80 Gin Glu Val Glu Leu Val Asn Val Thr Glu Asn Phe Asn Met Trp Lys 85 90 95 Asn Asn Met Val Glu Gin Met Hie Glu Asp lie lie Ser Leu Trp Asp 100 105 110 Gin Ser Leu Lys Prt. Cys Val Lys Leu Thr Pro Leu Cys Val Thr Leu 115 120 125 Aβn Cyβ Aβp Thr Leu Arg Aβn Thr Thr Aβn Thr Aβn Aβn Ser Thr Ala 130 135 140 Asn Asn Asn Ser Asn Ser Glu Gly Thr lie Lys Gly Gly Glu Met Lys 145 150 155 160 Asn Cys Ser Phe Asn lie Thr Thr Ser lie Arg Asp Lys Met Gin Lys 165 170 175 Glu Tyr Ala Leu Leu Val Lye Leu Asp lie Val Pro lie Aβp Aβn Aβp 180 185 190 Ser Thr Ser Tyr Arg Leu lie Ser Cys Asn Thr Ser Val lie Thr Gin 195 200 205 Ala Cys Pro Lys lie Ser Phe Glu Pro lie Pro lie Hie Tyr Cyβ Ala .210 215 220 Pro Ala Gly Phe Ala lie Leu Lys Cyβ Asn Aβp Lys Lys Phe Ser Gly 225 230 235 240 a. ■ a Gly Ser Cys Lys Asn Val Ser Thr Val Gin Cys Thr His Gly lie 245 250 255 Arg Pro Val Val Ser Thr Gin Leu Leu Leu Aβn Gly Ser Leu Ala Glu 260 265 270 Glu Glu Val Val lie Arg Ser Glu Aβn Phe Thr Asp Asn Ala Lys Thr 275 280 285 lie lie Val His Leu Asn Glu Ser Val Gin lie Asn Cyβ Thr Arg Pro 290 295 330 Aβn Tyr Asn Lys Arg Lye Arg lie Hie lie Gly Pro Gly Arg Ala Phe 305 310 315 320 Tyr Thr Thr Lye Asn lie lie Gly Thr lie Arg Gin Ala His Cyβ Aβn 325 330 335 Leu Ser Arg Ser Lye Trp Glu Aβn Thr Leu Lye Gin lie Val Thr Lye 340 345 350 Leu Arg Val Gin Phe Lys Asn Lys Thr lie Val Phe Asn Arg Ser Ser 355 360 365 Gly Gly Asp Pro Glu lie Val Met His Ser Phe Asn Cys Gly Gly Glu 370 375 380 Phe Phe Tyr Cys Aβn Thr Ser Pro Leu Phe Aβn Ser Thr Trp Asn Gly 385 390 395 400 Asn Aβn Thr Trp Aβn Aβn Thr Thr Gly Ser Aβn Aβn Aβn lie Thr Leu 405 410 415 Gin Cyβ Lye lie Lye Gin lie lie Aβn Met Trp Gin Glu Val Gly Lye 420 425 430 Ala Met Tyr Ala Pro Pro lie Glu Gly Gin lie Arg Cyβ Ser Ser Aβn 435 440 445 lie Thr Gly Leu Leu Leu Thr Arg Asp Gly Gly Lys Asp Thr Aβp Thr 450 455 460 Asn Asp Thr Glu lie Phe Arg Pro Gly Gly Gly Asp Met Arg Asp Asn 465 470 475 480 Trp Arg Ser Glu Leu Tyr Lys Tyr Lys Val Val Thr lie Glu Pro Leu 485 490 495 Gly Val Ala Pro Thr Lye Ala Lys Arg Arg Val Val Gin Arg Glu Lys 500 505 510 Arg Ala Ala lie Gly Ala Leu Phe Leu Gly Phe Leu Gly Ala Ala Gly 515 520 525 Ser Thr Met Gly Ala Ala Ser Val Thr Leu Thr Val Gin Ala Arg Leu 530 535 540 Leu Leu Ser Gly lie Val Gin Gin Gin Asn Asn Leu Leu Arg Ala lie 545 550 555 560 Glu Ala Gin Gin Hie Met Leu Gin Leu Thr Val Trp Gly lie Lye Gin 565 570 575 Leu Gin Ala Arg Val Leu Ala Val Glu Arg Tyr Leu Lys Aβp Gin Gin 580 585 590 Leu Leu Gly Phe Trp Gly Cyβ Ser Gly Lye Leu lie Cyβ Thr Thr Thr 595 600 605 Val Pro Trp Asn Ala Ser Trp Ser Aβn Lys Ser Leu Asp Asp lie Trp 610 615 620 Asn Asn Met Thr Trp Met Gin Trp Glu Arg Glu lie Asp Asn Tyr Thr 625 630 635 640 Ser Leu lie Tyr Ser Leu Leu Glu Lys Ser Gin Thr Gin Gin Glu Lye 645 650 655 Aβn Glu Gin Glu Leu Leu Glu Leu Aβp Lye Trp Ala Ser Leu Trp Aβn 660 665 670 Trp Phe Asp lie Thr Asn Trp Leu Trp Tyr lie Lys lie Phe lie Met 675 680 685 lie Val Gly Gly Leu Val Gly Leu Arg lie Val Phe Ala Val Leu Ser 690 695 700 lie Val Asn Arg Val Arg Gin Gly Tyr Ser Pro Leu Ser Leu Gin Thr 705 710 715 720 Arg Pro Pro Val Pro Arg Gly Pro Aβp Arg Pro Glu Gly He Glu Glu 725 730 735 Glu Gly Gly Glu Arg Asp Arg Asp Thr Ser Gly Arg Leu Val Hie Gly 740 745 750 Phe Leu Ala He He Trp Val Aβp Leu Arg Ser Leu Phe Leu Phe Ser 755 760 765 Tyr Hie Hie Arg Aβp Leu Leu Leu He Alε Ala Arg He Val Glu Leu 770 775 780 Leu Gly Arg Arg Gly Trp Glu Val Leu Lye Tyr Trp Trp Aβn Leu Leu 785 790 795 800 Gin Tyr Trp Ser Gin Glu Leu Lye Ser Ser Ala Val Ser Leu Leu Aβn 805 810 815 Ala Thr Ala He Ala Val Ala Glu Gly Thr Aβp Arg Val He Glu Val 820 825 830 Leu Gin Arg Ala Gly Arg Ala He Leu Hie He Pro Thr Arg He Arg 835 840 845 Gin Gly Leu Glu Arg Ala Leu Leu 850 855 (2) INFORMATION FOR SEQ ID NO:2: (i) SEQUENCE CHARACTER3TICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:2: Arg He Lys Gin He He Aβn Met Trp Gin Glu Val Gly Lye Ala Met 1 5 10 15 Tyr Ala (2) INFORMATION FOR SEQ ID NO:3: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (xi ) SEQUENCE DESCRIPTION: SEQ ID NO: 3 : Arg He Lye Gin Phe He Aβn Met Trp Gin Glu Val Gly Lye Ala Met 1 5 10 15 Tyr Ala (2) INFORMATION FOR SEQ ID NO:4: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:4: Arg He Lye Gin He He Aβn Met Trp Gin Lye Val Gly Lye Ala Met 1 5 10 15 Tyr Ala (2) INFORMATION FOR SEQ ID NO:5: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:5: Arg He Lye Glu He He Aβn Met Trp Gin Glu Val Gly Lys Ala Met 1 5 10 15 Tyr Ala (2) INFORMATION FOR SEQ ID NO:6: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO ( xi ) SEQUENCE DESCRIPTION: SEQ ID NO: 6 : Arg He Lys Gin He He Asn Met Trp Gin Glu Val Gly Lys Ala Met 1 5 10 15 Tyr Ala (2) INFORMATION FOR SEQ ID NO:7: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:7: Lys He Lys Gin He He Aβn Met Trp Gin Glu Val Gly Lye Ala Met 1 5 10 15 Tyr Ala (2) INFORMATION FOR SEQ ID NO:8: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:8: Arg He Lys Gin He He Aβn Met Trp Gin Xaa Val Gly Lys Ala Met 1 5 10 15 Tyr Ala (2) INFORMATION FOR SEQ ID NO:9: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 17 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (xi ) SEQUENCE DESCRIPTION: SEQ ID NO: 9 : Arg He Lye Gin He He Lye Met Val Ala Gly Arg Lys Ala He Tyr 1 5 10 15 Ala (2) INFORMATION FOR SEQ ID NO:10: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:10: Arg He Lys Gin He He Asn Met Trp Gin Arg Val Gly Gin Ala Met 1 5 10 15 Tyr Ala (2) INFORMATION FOR SEQ ID NO:11: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:11: His He Lys Gin He Val Asn Thr Trp Hiβ Lys Val Gly Lys Tyr Val 1 5 10 15 Tyr Leu (2) INFORMATION FOR SEQ ID NO:12: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acids (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (xi ) SEQUENCE DESCRIPTION: SEQ ID NO: 12 : His He Arg Gin He He Aβn Thr Trp Hiβ Lye Val Gly Lye Aβn Val 1 5 10 15 Tyr Leu (2) INFORMATION FOR SEQ ID NO:13: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 amino acidβ (B) TYPE: amino acid (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (xi) SEQUENCE DESCRIPTION: SEQ ID NO:13: Hiβ He Glu Gin He He Aβn Thr Trp Hiβ Lye Val Gly Lys Aβn Val 1 5 10 15 Tyr Leu

Claims: WHAT IS CLAIMED IS: 1. A method of detecting the presence of an antibody reactive with an HIV envelope protein in a biological sample, the method comprising contacting the sample with a peptomer comprising a plurality of peptide monomers, each comprising a sequence from a CD4 binding region of gpl20 from HTV; and detecting the formation of a peptomer-antibody complex. 2. The method of claim 1, wherein the peptomer is constructed from haloacetyl-derivatized peptide monomers. 3. The method of claim 1, wherein the HIV is HIV-1. 4. The method of claim 1, wherein each peptide monomer has a sequence consisting essentially of KIKQIINMWQEVGKAMYA (SEQ. ID. No. 7). 5. The method of claim 1, wherein the peptomer is bound to a solid surface. 6. The method of claim 1, wherein the sample is a blood sample. 7. A method of inducing antibodies against gpl20, the method comprising administering to a mammal an immunogenic composition comprising an immunogenically effective amount of a peptomer comprising a plurality of peptide monomers, each comprising a sequence from a CD4 binding region of gpl20 from HIV, and a pharmaceutically acceptable carrier which preserves the secondary structure of the peptomer. 8. The method of claim 7, wherein the mammal is a rabbit. 9. The method of claim 7, wherein the HIV is HIV-1. 10. The method of claim 7, wherein each peptide monomer has a sequence consisting essentially of KIKQIINMWQEVGKAMYA (SEQ. ID. No. 7). 11. The method of claim 7, wherein the peptomer is constructed from haloacetyl-derivatized peptide monomers. 12. The method of claim 7, wherein the immunogenic composition further comprises an adjuvant. 13. The method of claim 12, wherein the adjuvant is Ribi's adjuvant. 14. An antibody isolated from a mammal immunized according to the method of claim 7. 15. An immunogenic composition comprising an immunogenically effective amount of a peptomer comprising a plurality of peptide monomers, each comprising a sequence from a CD4 binding region of gpl20 from HTV, and a pharmaceutically acceptable carrier which preserves the secondary structure of the peptomer. 16. The composition of claim 15, wherein the HTV is HIV-1. 17. The composition of claim 15, wherein each peptide monomer has a sequence consisting essentially of KIKQIINMWQEVGKAMYA (SEQ. ID. No. 7). 18. The composition of claim 15, wherein the peptomer comprises haloacetyl-derivatized peptide monomers. 19. The composition of claim 15, further comprising an adjuvant. 20. The composition of claim 19, wherein the adjuvant is Ribi's adjuvant. 21. A composition comprising a peptomer comprising a plurality of peptide monomers, each peptide monomer comprising a sequence from a CD4 binding region of gpl20 from HTV. 22. The composition of claim 21, wherein each peptide monomer consists essentially of KIKQIINMWQEVGKAMYA (SEQ. ID. No. 7). 23. The composition of claim 21, wherein the peptomer is constructed from haloacetyl derivatized peptide monomers. 24. The composition of claim 21, wherein the peptomer is prepared such that solubility in aqueous solution is maintained. 25. The composition of claim 24, wherein the peptomer has a solubility of at least about lmg/ml. 26. The composition of claim 21, which is a spermicidal gel. 27. A vaccine comprising an immunogenically effective amount of a peptomer comprising a plurality of peptide monomers, each comprising a sequence from a CD4 binding region of gpl20 from HTV, and a pharmaceutically acceptable carrier which preserves the secondary structure of the peptomer. 28. The vaccine of claim 27, wherein the HTV is HIV-1. 29. The vaccine of claim 27, wherein each peptide monomer has a sequence consisting essentially of KIKQIINMWQEVGKAMYA (SEQ. ID. No. 7). 30. The vaccine of claim 27, wherein the peptomer is constructed from haloacetyl derivatized peptide monomers. 31. The vaccine of claim 27, further comprising a second peptomer comprising a plurality of peptide monomers, each comprising a sequence from a CD4 binding region of gpl20 from HIV, the peptomer being prepared such that solubility in aqueous solutions is maintained. 32. The vaccine of claim 31, wherein the second peptomer has a solubility of at least about lmg/ml. 33. A composition comprising a peptide having a sequence from a CD4 binding region of gpl20 from HIV and a detergent, such that the peptide forms an α- helix. 34. The composition of claim 33, wherein each peptide has a sequence consisting essentially of KIKQIINMWQEVGKAMYA (SEQ. ID. No. 7).

Inventors: HARRIS-KELSON TRACY A, ROBERT-GUROFF MARJORIE, ROBEY FRANK A, HARRIS-KELSON, TRACY, A., ROBERT-GUROFF, MARJORIE, ROBEY, FRANK, A.
Applicants: US HEALTH, THE GOVERNMENT OF THE UNITED STATES OF AMERICA, RE
Application year: 1995
Main classification: G01N33
IPC codes: A61K39, C07K1, C07K14, G01N33