Cell-permeable peptide inhibitors of the JNK signal...

Details Cell-permeable peptide inhibitors of the JNK signal... Cell-permeable peptide inhibitors of the JNK signal...

2003-01-09

2009-12-22

Stucker, Jeffrey (Department: 1649)

Drug, bio-affecting and body treating compositions

Designated organic active ingredient containing

Peptide containing doai

C514S012200, C530S326000, C530S325000, C530S324000

Reexamination Certificate

active

07635681

ABSTRACT:
The invention provides cell-permeable peptides that selectively block the branch of the JNK signaling pathway controlled by the islet-brain (IB) proteins. The provided cell-permeable peptides block the binding of intermediate kinases in the c-Jun amino terminal kinase (JNK) signaling pathway, thereby decreasing the downstream effects of c-Jun amino terminal kinase (JNK).

REFERENCES:
patent: 4631211 (1986-12-01), Houghten
patent: 6348185 (2002-02-01), Piwnica-Worms
patent: 6653443 (2003-11-01), Zhang et al.
patent: WO 94/04686 (1994-03-01), None
patent: WO 98/47913 (1998-10-01), None
patent: WO 98/49188 (1998-11-01), None
patent: WO 99/50282 (1999-10-01), None
patent: WO 96/58561 (1999-11-01), None
patent: WO 01/27268 (2001-04-01), None
patent: WO 02/81504 (2002-10-01), None
Waldmeier et al (2006). Biochemical Pharmacology. 72, 1197-1206.
Mayer (1997).. J. Cell Science. 1253-1263.
Rickles et al (1995). PNAS. 92, 10909-10913.
Negri et al. Diabetes, A Journal of the American Diabetes Association, vol. 50, Supplement 2, Abstract Book for the 61stScientific Sessions, Pennsylvania Convention Center, Jun. 2001, p. A294.
Diabetes, A Journal of the American Diabetes Association, Abstract Book, 61st Scientific Sessions, Pennsylvania Convention Center, Philadelphia, PA, 50 (Suppl 2), Jun. 2001.
Abaza et al. “Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization: demonstration with region 94-100 (antigenic site 3) of myoglobin” J. Protein Chem. 11(5), pp. 433-444 (1992).
Agrawal et al. “Promiscuous binding nature of SH3 domains to their target proteins”, Protein Pept. Lett., 9(3):185-193 (2002).
Bonny et al. “Cell-permeable peptide inhibitors of JNK: novel blockers of beta-cell death”, Diabetes, 50(1):77-82 (2001).
Borsello et al. “A peptide inhibitor of c-Jun N-terminal kinase protects against excitotoxicity and cerebral ischemia”, Nat Med. 9(9), pp. 1180-1186 (2003).
Creighton, T. Encyclopedia of Molecular Biology, John Wiley and Sons, Inc. New York, pp. 2027-2033 (1999).
Fawell et al. “Tat-mediated delivery of heterologous proteins into cells” Proc. Natl. Acad. Sci. USA. 91(2), pp. 664-668 (1994).
GenBank Database Accession No. PH0878, May 1997.
Huq et al. “Specific recognition of HIV-1 TAR RNA by a D-Tat peptide”, Nat Struct Biol. 4(11), pp. 881-882 (1997).
Houghten, “General method for the rapid solid-phase synthesis of large numbers of peptides: specificity of antigen-antibody interaction at the level of individual amino acids”, Proc. Natl. Acad. Sci. USA, 82(15):5131-5135 (1985).
International Search Report for PCT/IB03/00332, mailing date: Jul. 19, 2004.
Kishan et al. “SH3 -like fold proteins are structurally conserved and functionally divergent”, Curr. Protein Pept. Sci., 6(2):143-150 (2005).
Li, S. “Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction”, Biochem. J., 390(Pt 3):641-653 (2005).
Mayer et al.: “SH3 domains: complexity in moderation”, J. Cell Science, vol. 114(7), pp. 1253-1263, 1997.
Moulin et al. “Islet-brain (IB)/JNK-interacting proteins (JIPs): future targets for the treatment of neurodegenerative diseases?”, Curr. Neurovasc. Res., 1(2):111-127 (2004).
Rickles et al. “Phage display selection of ligand residues important for Src homology 3 domain binding specificity”, 92(24): 10909-10913 (1995).
Stevens et al., “Peptide length preferences for rat and mouse MHC class I molecules using random peptide libraries”, Eur. J. Immunol , 28(4):1272-1279 (1998).
Stevens et al., “Efficient generation of major histocompatibility complex class I-peptide complexes using synthetic peptide libraries”, J. Biol. Chem., 273(5):2874-2884 (1998).
Vives et al. “A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus”, J. Biol. Chem., 272(25):16010-16017 (1997).

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