Stable macroscopic membranes formed by self-assembly of amphiphi

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

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514 12, 514 13, 530300, 530324, 530325, 530326, 530327, 530350, A61K 708, A61K 1400, C07K 3810, C07K 3816

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active

056704836

ABSTRACT:
Described herein is the self-assembly of amphiphilic peptides, i.e., peptides with alternating hydrophobic and hydrophilic residues, into macroscopic membranes. The membrane-forming peptides are greater than 12 amino acids in length, and preferably at least 16 amino acids, are complementary and are structurally compatible. Specifically, two peptides, (AEAEAKAK).sub.2 (ARARADAD).sub.2, were shown to self-assemble into macroscopic membranes. Conditions under which the peptides self-assemble into macroscopic membranes and methods for producing the membranes are also described. The macroscopic membranes have several interesting properties: they are stable in aqueous solution, serum, and ethanol, are highly resistant to heat, alkaline and acidic pH, chemical denaturants, and proteolytic digestion, and are non-cytotoxic. The membranes are potentially useful in biomaterial applications such as slow-diffusion drug delivery systems, artificial skin, and separation matrices, and as experimental models for Alzheimer's disease and scrapie infection. The sequence of the peptide, EAK16, was derived from a putative Z-DNA binding protein from yeast, called zuotin. The cloning and characterization of the ZUO1 gene are also described.

REFERENCES:
patent: 5080936 (1992-01-01), Cerwen
Smith,G.G. et al.; J. Pharm. Sci. 65:727-732 (1976).
Physician's Desk Reference 47th Edition, Medical Economics Data, Montvale, NJ., 1993, p. 2598.
WPI Accession No. 92-313678/38 (abstract of JP 4-221394).
WPI Accession No. 92-313679/38 (abstract of JP 4-221395).
Zhang et al., "Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae", The EMBO J. 11(10):3787-3796 (1992).
Osterman, D.G. and Kaiser, E.T., "Design and Characterization of Peptides with Amphiphilic .beta.-Strand Structures", J. Cell. Biochem. 29:57-72 (1985).
Brack, A. and Orgel, L.E., ".beta.structures of alternating polypeptides and their possible prebiotic significance", Nature 256:383-387 (1975).
Brack, A. and Caille, A., "Synthesis and .beta.-Conformation of Copolypeptides with Alternating Hydrophilic and Hydrophobic Residues":, Int. J. Peptide Protein Res. 11:128-139 (1978).
Brack, A. and Barbier, B., "Early Peptidic Enzymes", Adv. Spac. Res. 9(6): (6)83-(6)87 (1989).
Marqusee S. and Baldwin, R.L., "Helix stabilization by Glu.sup.-. . . Lys.sup.+ salt bridges in short peptides of de novo design", Proc. Natl. Acad. Sci. USA 84:8898-8902 (1987).
Marqusee, S., et al., "Unusually stable helix formation in short alanine-based peptides", Proc. Natl. Acad. Sci. USA 86:5286-5290 (1989).
Padmanabhan, S., et al., "Relative helix-forming tendencies of nonpolar amino acids", Nature 344:268-270 (1991).
Seipke, G., et al., "Synthesis and Properties of Alternating Poly(Lys-Phe) and Comparison with the Random Copolymer Poly(Lys.sup.51, Phe.sup.49)", Biopolymers 13:1621-1633 (1974).
St. Pierre, S., et al., "Conformational Studies of Sequential Polypeptides Containing Lysine and Tyrosine", Biopolymers 17:1837-1848 (1978).
Peggion, E., et al., "Conformational Studies on Polypeptides. The Effect of Sodium Perchlorate on the Conformation of Poly-L-lysine and of Random Copolymers of L-Lysine and L-Phenylalanine in Aqueous Solution",Biopolymers 11:633-643 (1972).
Trudelle, Y., "Conformational study of the sequential (Tyr-Glu).sub..eta. copolymer in aqueous solution", Polymer 16:9-15 (1975).
Rippon, W.B., et al., "Spectroscopic Characterization of Poly(Glu-Ala)", J. Mol. Biol. 75:369-375 (1973).
Gay, N.J., et al., "A leucine-rich repeat peptide derived from the Drosophila Toll receptor forms extended filaments with a .beta.-sheet structure", FEBS 291(1):87-91 (1991).
Hilbich, C., et al., "Aggregation and Secondary Structure of Synthetic Amyloid .beta.A4 Peptides of Alzheimer's Disease", J. Mol. Biol. 218:149-163 (1991).
Halverson, K., "Molecular Determinants of Amyloid Deposition in Alzheimer's Disease: Conformational Studies of Synthetic .beta.-Protein Fragments", Biochemistry 29:2639-2644 (1990).
Gasset, M., et al., "Pertubation of the secondary structure of the scrapie prion protein under conditions that alter infectivity", Proc. Natl. Acad. Sci. USA 90:1-5 (1993).
Lizardi, P.M., "Genetic Polymorphism of Silk Fibroin Studied by Two-Dimensional Translation Pause Fingerprints", Cell 18:581-589 (1979).
Thomas, E.L., "Gigamolecules in Flatland", Science 259:43-45 (1993).
Stupp, S.I., "Synthesis of Two-Dimensional Polymers", Science 259:59-63 (1993).
Gulik-Krzywicki, T., et al., "Electron microscopic study of supramolecular liquid crystalline polymers formed by molecular recognition-directed self-assembly from complementary chiral components", Proc. Natl. Acad. Sci. USA 90:163-167 (1993).

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