Methods and compositions for inhibiting GRB7

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

Reexamination Certificate

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C514S011400, C514S013800, C514S014800, C514S015800

Reexamination Certificate

active

10013815

ABSTRACT:
The invention provides methods and compositions for treating subjects using Grb7 antagonists. Specifically disclosed are Grb7 antagonists that bind selectively to Grb7 and interfere with the ability of Grb7 to bind to its native ligands. These compositions are useful in the prevention and treatment of disorders characterized by abnormal interaction of Grb7 with its native ligands (e.g., ErbB2).

REFERENCES:
patent: 5710129 (1998-01-01), Lynch et al.
patent: 6001583 (1999-12-01), Margolis
patent: WO 97/08193 (1997-03-01), None
Gura (Science, 1997, 278:1041-1042).
Jain (Sci. Am., 1994, 271:58-65).
Curti (Crit. Rev. in Oncology/Hematology, 1993, 14:29-39).
Bowie et al (Science, 1990, 257:1306-1310).
Burgess et al ( J of Cell Bio. 111:2129-2138, 1990).
, Bork (Genome Research, 2000, 10:398-400).
Gram, et al., “Identification of phosphopeptide ligands for the Src-homology 2 (SH2) domain of Grb2 by phage display,” 1997, Eur. J. Biochem., vol. 246, pp. 633-637.
Müller, et al., “Rapid Identification of Phosphopeptide Ligands for SH2 Domains,” 1996, The Journal of Biological Chemistry, vol. 271, No. 28, pp. 16500-16505.
Schoepfer, et al., Highly Potent Inhibitors of the Grb2-SH2 Domain, 1999, Bioorganic & Medicinal Chemistry Letters 9, pp. 221-226.
Ettmayer, et al., “Structural and Conformational Requirements for High-Affinity Binding to the SH2 Domain of Grb2,” 1999, J. Med. Chem., vol. 42, pp. 971-980.
Furet, et al., “Structure-Based Design and Synthesis of High Affinity Tripeptide Ligands of the Grb2-SH2 Domain,” 1998, J. Med. Chem., vol. 41, pp. 3442-3449.
Gay, et al., “Selective Grb2 SH2 Inhibitors as Anti-Ras Therapy,” 1999, Int. J. Cancer, vol. 83, pp. 235-241.
Gay, et al., “Effect of Potent and Selective Inhibitors of the Grb2 SH2 Domain on Cell Motility,” 1999, The Journal of Biological Chemistry, vol. 274, No. 33, pp. 23311-23315.
Raheul, et al., “Structural Basis for the High Affinity of Amino-Aromatic SH2 Phosphopeptide Ligands,” 1998, J. Mol. Biol., vol. 279, pp. 1013-1022.
Schoepfer, et al., “Structure-Based Design of Peptidomimetic Ligands of the Grb2-SH2 Domain,” 1998, Bioorganic & Medicinal Chemistry Letters 8, pp. 2865-2870.
Oligino, et al., “Nonphosphorylated Peptide Ligands for the Grb2 Src Homology 2 Domain,” 1997, The Journal of Biological Chemistry, vol. 272, No. 46, pp. 29046-29052.
Burgess, et al., “Possible Dissociation of the Heparin-binding and Mitogenic Activities of Heparin-binding (Acidic Fibroblast) Growth Factor-1 from Its Receptor-binding Activities by Site-directed Mutagenesis of a Single Lysine Residue,” 1990, The Journal of Cell Biology, vol. 111, pp. 2129-2138.
Lazar, et al., “Transforming Growth Factor α: Mutation of Aspartic Acid 47 and Leucine 48 Results in Different Biological Activities,” 1988, Molecular and Cellular Biology, pp. 1247-1252.
Tao, et al., “Studies of Aglycosylated Chimeric Mouse-Human IgG,” 1989, The Journal of Immunology, vol. 143, No. 8, pp. 2595-2601.
Gillies, et al., “Antigen binding and biological activities of engineered mutant chimeric antibodies with human tumor specificities”, 1990, Hum. Antibod. Hybridomas, vol. 1, No. 1, pp.47-54.
Lou, et al., “Solution Structure and Dynmaics of G1TE, a Nonphosphorylated Cyclic Peptide Inhibitor for the Grb2 SH2 Domain,” 1999, Archives of Biochemistry and Biophysics, vol. 372, No. 2, pp. 309-314.
Burke, Jr., et al., “Monocarboxylic-Based Phosphotyrosyl Mimetics in the Design of GRB2 SH2 Domain Inhibitors,” 1999, Bioorganic & Medicinal Chemistry Letters 9, pp. 347-352.
Long., et al., “Structural Requirements for Tyr in the Consensus Sequence Y-E-N of a Novel Nonphosphorylated Inhibitor to the Grb2-SH2 Domain,” 1999, Biochemical and Biophysical Research Communications, vol. 264, pp. 902-908.
Yao, et al., “Potent Inhibition of Grb2 SH2 Domain Binding by Non-Phophate-Containing Ligands,” 1999, J. Med. Chem., vol. 42, pp. 25-35.
Ye, et al., “L-O-(2-Malonyl)tyrosine: A New Phosphotyrosyl Mimetic for the Preparation of Src Homology 2 Domain Inhibitory Peptides,” 1995, J. Med. Chem., vol. 38, pp. 4270-4275.
Hart, et al., “Potent Inhibitory Ligands of the GRB2 SH2 Domain from Recombinant Peptide Libraries,” 1999, Cell. Signal., vol. 11, No. 6, pp. 453-464.
Long, et al., “Significant Compensatory Role of Position Y-2 Conferring High Affinity to Non-Phosphorylated Inhibitors of GRB2 SH2 Domain,” 1999, Bioorganic & Medicinal Chemistry Letters 9, pp. 2267-2272.
Long, et al., “High affinity nonphosphorylated cyclic peptide inhibitors of Grb2-SH2/growth factor receptor interactions,” Book Title: “Peptides for the New Millennium,” Book Author/Editor: Greg B. Field; James B. Tam and George Barany; Book Publisher: Kulwer Academic Publishers, Netherlands, pp. 567-570, 2000.
Garcia-Echeverria, et al., Mapping the X(+1) binding site of the Grb2-SH2 domain with alpha, alpha-distributed cyclic alpha-amino acids, 1999, Bioorg. Med. Chem. Lett., vol. 9, No. 20, pp. 2915-2920 Abstract.
Caravatti, et al., “Structure-based design of a non-peptide antagonist of the SH2 domain of GRB2,” Bioorg. Med. Chem. Lett., vol. 9, No. 14, pp. 1973-1978 Abstract.
Furet, et al., “Discovery of 3-aminobenzyloxcarbonyl as an N-terminal group conferring high affinity to the minimal phosphopeptide sequence recognized by the Grb2-SH2 domain,” 1997, J. Med. Chem., vol. 40, No. 22, pp. 3551-3556 Abstract.
Garcia-Echeverria, et al., Potent antagonists of the SH2 domain of Grb2: optimization of the X+1 position of 3-amino-Z-Tyr(PO3H2)-X+1-Asn-NH2., 1998, J. Med. Chem., vol. 41, No. 11, pp. 1741-1744 Abstract.
Pero, et al., “Identification of Novel Non-phosphorylated Ligands, Which Bind Selectively to the SH2 Domain of Grb7,” The Journal of Biological Chemistry, Apr. 5, 2002, vol. 277, No. 14, pp. 11918-11926.
Janes et al., Structural determinants of the interaction between the erbB2 receptor and the Src homology 2 domain of Grb7. J Biol Chem. Mar. 28, 1997;272(13):8490-7.
Oligino et al., Nonphosphorylated peptide ligands for the Grb2 Src homology 2 domain. J Biol Chem. Nov. 14, 1997;272(46):29046-52.
Keegan et al., Use of the two hybrid system to detect the association of the protein-tyrosine-phosphatase, SHPTP2, with another SH2-containing protein, Grb7. Oncogene. Apr. 4, 1996;12(7):1537-44.
PCT/US01/47400 International Search Report; Mailing Date—Nov. 29, 2002.
PCT/US01/47400 Written Opinion; Mailing Date—Aug. 11, 2003.
PCT/US01/47400 International Preliminary Exmination Report; Mailing Date—Apr. 15, 2004.

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