β-peptides

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

Reexamination Certificate

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C525S054110, C435S106000, C436S090000

Reexamination Certificate

active

08008262

ABSTRACT:
β-peptide regions of polypeptides can serve as structural mimics of α-helices in wild type proteins. Because α-helices of one protein often bind to a target protein in a biological pathway, a polypeptide that contains a helical β-peptide region can be used to disrupt this type of protein-protein binding. As a result, polypeptides that contain a helical β-peptide region can be used to treat conditions involving this type of protein-protein binding, such as viral infections and cell proliferation.

REFERENCES:
patent: WO 97/47593 (1997-12-01), None
Arvidsson, 2001, Chem. Commun., 649-650.
Hart, 2003, Journal of American Chemical Society, 125, 4022-4023.
Neuman de Vegvar, 2003, Journal of Virology, 77, 11125-11138.
Seebach, et al. “Biological and Pharmacokinetic Studies with β-Peptides,”Chimia 5., (1998), pp. 734-739, Neue Schweizerische Chemische Gsellschaft.
Seebach, et al. “β-Peptides: Synthesis by Arndt-Eistert Homologation with Concomitant Peptide Coupling. Structure Determination by NMR and CD Spectroscopy and by X-Ray Crystallography. Helical Secondary Structure of a β-Hexapeptide in Solution and Its Stability towards Pepsin,”Helvetica Chimica Acta. vol. 79, (1996), pp. 913-941.
Frackenpohl, et al. “The Outstanding Biological Stability of β- and γ-Peptides toward Proteolytic Enzymes: an In Vitro Investigation with Fifteen peptidases,”Chembiochem, 2001, 2, 445-455, Wiley-VCH-Verlag GmbH, D-69451 Weinheim, 2001.
Arvidsson, Per, et al., “Design, Machine Synthesis, and NMR-solution Structure of a β-Heptapeptide Forming a Salt-Bridge Stabilized 314-Helix in Methanol and in Water,” Chemical Communications, pp. 649-650, 2001.
Cheng, Richard P. et al., “De Novo Design of a Monomeric Helical β-Peptide Stabilized by Electrostatic Interactions,” Journal of the American Chemical Society, 123(21), pp. 5162-5163, 2001.
Gademann, Karl et al., “Peptide Folding Induces High and Selective Affinity of a Linear and Small β-Peptide to the Human Somatostatin Receptor 4,” Journal of Medicinal Chemistry, 44(15), pp. 2460-2468, 2001.
Gellman et al., “Foldamers: A Manifesto,” Accounts of Chemical Research, vol. 31, No. 4, 1998, pp. 173-180.
Hart, Scott A., et al., “Helix Macrodipole Control of β3-Peptide 14-Helix Stability in Water,” Journal of the American Chemical Society, 125(14), pp. 4022-4023, 2003.
Kritzer, Joshua A., et al., “Helical β-Peptide Inhibitors of the p53-hDM2 Interaction,” Journal of the American Chemical Society, 126(31), pp. 9468-9469, 2004.
Kritzer, Joshua A., et al., “Relationship between Side Chain Structure and 14-Helix Stability of 83-Peptides in Water,” Journal of the American Chemical Society, 127(1), pp. 167-178, 2005.
Kritzer, Joshua A., et al., “Solution Structure of a β-Peptide Ligand for hDM2,” Journal of the American Chemical Society, 127, pp. 4118-4119, 2005.
Kritzer, Joshua A., et al., “β-Peptides as Inhibitors of Protein-Protein Interactions,” Bioorganic & Medicinal Chemistry, 13()), pp. 11-16, 2004.
Murray, Justin K., et al., “Application of Microwave Irradiation to the Synthesis of 14-Helical β-Peptides,” Organic Letters, vol. 7, No. 8, pp. 1517-1520, 2005.
Raguse, Tami L., et al., Environment-Independent 14-Helix Formation in Short β-Peptides: Striking a Balance between Shape Control and Functional Diversity, Journal of the American Chemical Society, 125(19), pp. 5592-5593, 2003.
Search Report mailed Sep. 15, 2006 in PCT/US2005/013570 (filed Apr. 21, 2005).

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