Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Fusion protein or fusion polypeptide
Reexamination Certificate
2007-04-12
2010-10-12
Parkin, Jeffrey S. (Department: 1648)
Drug, bio-affecting and body treating compositions
Antigen, epitope, or other immunospecific immunoeffector
Fusion protein or fusion polypeptide
C424S188100, C424S208100
Reexamination Certificate
active
07811578
ABSTRACT:
Described herein are chimeric peptides comprising a soluble trimeric coiled-coil and all or a portion of the N-peptide region of HIV gp41. These molecules are stable, trimeric coiled-coils that inhibit HIV entry into cells, such as human cells. Such peptides can be further assessed to demonstrate their ability to serve as potent anti-HIV therapeutic molecules and thus, as therapeutic molecules or drugs.
REFERENCES:
patent: 5444044 (1995-08-01), Jiang et al.
patent: 5464933 (1995-11-01), Bolognesi et al.
patent: 5656480 (1997-08-01), Wild et al.
patent: 5780221 (1998-07-01), Schumacher et al.
patent: 5840843 (1998-11-01), Jiang et al.
patent: 6150088 (2000-11-01), Chan et al.
patent: 6506554 (2003-01-01), Chan et al.
patent: 6747126 (2004-06-01), Eckert et al.
patent: 6818740 (2004-11-01), Eckert et al.
patent: 6841657 (2005-01-01), Eckert et al.
patent: 7053179 (2006-05-01), Root et al.
patent: 7226598 (2007-06-01), Eckert et al.
patent: 7402396 (2008-07-01), Chan et al.
patent: 7504224 (2009-03-01), Root et al.
patent: 2001/0047080 (2001-11-01), Root et al.
patent: 2002/0077284 (2002-06-01), Eckert et al.
patent: 2003/0082525 (2003-05-01), Root et al.
patent: 2003/0099935 (2003-05-01), Chan et al.
patent: 2004/0044183 (2004-03-01), Eckert et al.
patent: 2004/0213801 (2004-10-01), Wild et al.
patent: 2005/0053917 (2005-03-01), Chan et al.
patent: 2005/0221294 (2005-10-01), Eckert et al.
patent: 2006/0014139 (2006-01-01), Root et al.
patent: WO 94/02505 (1994-02-01), None
patent: WO 96/40191 (1996-12-01), None
patent: WO 98/32848 (1998-07-01), None
patent: WO 00/06599 (2000-02-01), None
patent: WO 00/40616 (2000-07-01), None
patent: WO 01/03723 (2001-01-01), None
patent: WO 01/44286 (2001-06-01), None
patent: WO 02/24735 (2002-03-01), None
patent: WO 02/24735 (2002-03-01), None
Manchester, M., et al., 1994, Identification of temperature-sensitive mutants of the human immunodeficiency virus type 1 protease through saturation mutagenesis, J. Biol. Chem. 269(10):7689-7695.
Cao, J., et al., 1993, Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein, J. Virol. 67(5):2747-2755.
Moschella, F., et al., Administration of different antigenic forms of altered peptide ligands derived from HIV RTase influences their effects on T helper cell activation, Human Immunol. 64:1-8.
Eckert, D.M., and Kim, P.S., “Design of Potent Inhibitors of HIV-1 Entry from the gp41 N-peptide Region,”PNAS, 98(20):11187-11192 (Sep. 25, 2001).
Chen, et al., “Mutations in the leucine zipper-like heptad repeat sequence of Human Immunodeficiency Virus Type 1 gp41 Dominantly Interfere with Wild-Type Virus Infectivity,”J. of Virology, 72(6): 4765-4774 (1998).
Kliger et al., “Inhibition of HIV-1 Entry Before gp41 Folds into its Fusion-Active Conformation,”J. of Mol. Biol., 295: 163-168 (2000).
Bahbouhi, B., et al., “Effects of L-and D-REKR Amino Acid-Containing Peptides on HIV and SIV Envelope Glycoprotein Precursor Maturation and HIV and SIV Replication,”Biochem. J. 366(Pt. 3):863-872 (2002).
Baum, Rudy, “Virus-cell Fusion Targeted for Drug Development,” C&EN (May 13, 1996).
Benkirane, M., et al., “Antigenicity and Immunogenicity of Modified Synthetic Peptides Containing D-Amino Acid Residues. Antibodies to a D-Enantiomer Do Recognize the Parent L-Hexapeptide and Reciprocally,” J. Biol. Chem. 268(35): 26279-26285 (1993).
Bernstein, H.B., et al., “Oligomerization of the Hydrophobic Heptad Repeat of gp41,”Journal of Virology, 69(5):2745-2750 (1995).
Blacklow, Stephen C., et al., “A Trimeric Subdomain of the Simian Immunodeficiency Virus Envelope Glycoprotein,”Biochemistry, 34(46): 14955-14962 (1995).
Blake, James and Li, Choh Hao, “Adrenocorticotropin. 47. Synthesis and Biological Activity of Adrenocorticotropic Peptides Modified at the Tryptophan Position,”J. Medicinal Chem. 18(4):423-426 (1975).
Borchardt, Allen et al., “Small Molecule-dependent genetic selection in stochastic nanodroplets as a means of detecting protein-ligand interactions on a large scale,”Chem. &Biol. 4(12):961-968 (1997).
Bowie, J.U., et al., “Deciphering the Message in Protein Sequences: Tolerance to Amino Acid Substitutions,”Science, 247: 1306-1310 (1990).
Bullough, Per A. et al., “Structure of influenza haemagglutinin at the pH of membrane fusion,”Nature 371:37-43 (1994).
Buttó, C., et al., “Dual infection with different strains of the same HIV-1 subtype”, AIDS, vol. II, No. 5:694-696 (1997).
Caffrey, Michael et al., “Three-dimensional solution structure of the 44kDa ectodomain of SIV gp41,”EMBO J. 17(16):4572-4584 (1998).
Cao, Jie et al., “Effects of Amino Acid Changes in the Extracellular Domain of the Human Immunodeficiency Virus Type 1 gp41 Envelope Glycoprotein,”J. Virology 67(5):2747-2755 (1993).
Chabala, John C., “Solid-phase combinatorial chemistry and novel tagging methods for identifying leads,”Curr. Opin. Biotech. 6:632-639 (1995).
Chakrabartty, Avijit et al., “Aromatic Side-Chain Contribution to Far-Ultraviolet Circular Dichroism of Helical Peptides and Its Effect on Measurement of Helix Propensities,”Biochemistry 32:5560-5565 (1993).
Chambers, Philip, et al., “Heptad Repeat Sequences are Located Adjacent to Hydrophobic Regions in Several Types of Virus Fusion Glycoproteins,”Journal of General Virology, 71:3075-3080 (1990).
Chan, D.C. and Kim, P.S., “HIV Entry and Its Inhibition,”Cell 93:681-684 (1998).
Chan, David C., et al., “Core Structure of gp41 from the HIV Envelope Glycoprotein,”Cell 89:263-273 (1997).
Chan, D.C., et al., “Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target,”Proc. Natl. Sci. USA, 95:15613-15617 (1998).
Chang, Ding-Kwo, et al., “Proline Affects Oligomerization of a Coiled Coil by Inducing a Kink in a Long Helix,”Journal of Structural Biology, 128:270-279 (1999).
Chen, Benjamin K. et al., “Distinct Modes of Human Immunodeficiency Virus Type 1 Proviral Latency Revealed by Superinfection of Nonproductively Infected Cell Lines with Recombinant Luciferase-Encoding Viruses,”J. Virology 68(2):654-660 (1994).
Chen, Charlie L. et al., “One Bead-One Compound Combinatorial Peptide Library: Different Types of Screening,”Methods in Enzymology 267:211-219 (1996).
Chen, Chin-Ho et al., “A Molecular Clasp in the Human Immunodeficiency Virus (HIV) Type 1 TM Protein Determines the Anti-HIV Activity of gp41 Derivatives:Implication for Viral Fusion,”J. Virology 69(6):3771-3777 (1995).
Chen, Yee-Hsiung et al., “Determination of the Helix and β Form of Proteins in Aqueous Solution by Circular Dichroism,”Biochemistry 13(16):3350-3359 (1974).
Cole, James L. and Garsky, Victor M., “Thermodynamics of Peptide Inhibitor Binding to HIV-1 gp41,”Biochemistry 40:5633-5641 (2001).
Corigliano-Murphy, M.A., et al., “Synthesis and Properties of an All-D Model Ribonuclease S-Peptide,” Int. J. Pep. Prot. Res. 25:225-231 (1985).
Delwart, Eric L., et al., “Retroviral Envelope Glycoproteins Contain a ‘Leucine Zipper’-like Repeat,”AIDS Research and Human Retroviruses, 6(6):703-706 (1990).
Doering Don S. and Matsudaira, Paul, “Cysteine Scanning Mutagenesis at 40 of 76 Positions in Villin Headpiece Maps the F-Actin Binding Site and Structural Features of the Domain,”Biochemistry 35:12677-12685 (1996).
Dutch, Rebecca Ellis et al., “Paramyxovirus Fusion Protein: Characterization of the Core Trimer, a Rod-Shaped Complex with Helices in Anti-Parallel Orientation,”Virology 254:147-159 (1999).
Eckert, D.M. and Kim, P.S., “Mechanisms of Viral Membrane Fusion and Its Inhibition,” Annu. Rev. Biochem., 70:777-810 (2001).
Eckert, Debra M. et al., “Crystal Structur
Eckert Debra M.
Kim Peter S.
Suntoke Tara R.
Hamilton Brook Smith & Reynolds P.C.
Parkin Jeffrey S.
Whitehead Institute for Biomedical Research
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