Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues – 15 to 23 amino acid residues in defined sequence
Reexamination Certificate
2007-12-12
2011-11-22
Steele, Amber D. (Department: 1654)
Chemistry: natural resins or derivatives; peptides or proteins;
Peptides of 3 to 100 amino acid residues
15 to 23 amino acid residues in defined sequence
C536S023100, C506S014000, C435S005000
Reexamination Certificate
active
08063178
ABSTRACT:
Trp cage binding domains polypeptides are disclosed. The Trp cage binding domains have the generic formulae of SEQ ID NO: 2, 7, 10 or 11. They can be efficiently produced and screened using phage display technology.
REFERENCES:
patent: 5096815 (1992-03-01), Ladner et al.
patent: 5223409 (1993-06-01), Ladner et al.
patent: 5403484 (1995-04-01), Ladner et al.
patent: 5407911 (1995-04-01), Yamamoto et al.
patent: 5571698 (1996-11-01), Ladner et al.
patent: 5627024 (1997-05-01), Maruyama et al.
patent: 5658727 (1997-08-01), Barbas et al.
patent: 5667988 (1997-09-01), Barbas et al.
patent: 5738996 (1998-04-01), Hodges et al.
patent: 5750373 (1998-05-01), Garrard et al.
patent: 5759817 (1998-06-01), Barbas
patent: 5770356 (1998-06-01), Light, II et al.
patent: 5780279 (1998-07-01), Matthews et al.
patent: 5824483 (1998-10-01), Houston, Jr. et al.
patent: 5837500 (1998-11-01), Ladner et al.
patent: 5864009 (1999-01-01), Vlasuk et al.
patent: 5969108 (1999-10-01), McCafferty et al.
patent: 6492138 (2002-12-01), McGlade et al.
patent: 6734160 (2004-05-01), Friedman et al.
patent: 6743778 (2004-06-01), Kohno
patent: 6746838 (2004-06-01), Choo et al.
patent: 6773911 (2004-08-01), Penninger et al.
patent: 6835557 (2004-12-01), Weissman
patent: 6855804 (2005-02-01), Paul et al.
patent: 6866997 (2005-03-01), Choo et al.
patent: 6906176 (2005-06-01), Ley et al.
patent: 6914123 (2005-07-01), Cochran et al.
patent: 7060682 (2006-06-01), Darnell et al.
patent: 7183062 (2007-02-01), Parkar et al.
patent: 7229777 (2007-06-01), Cochran et al.
patent: 7339039 (2008-03-01), Darnell et al.
patent: 7365154 (2008-04-01), Shealy et al.
patent: 7608681 (2009-10-01), Dennis et al.
patent: 2002/0012909 (2002-01-01), Plaskin et al.
patent: 2002/0069422 (2002-06-01), Fransen
patent: 2002/0076728 (2002-06-01), Maclennan et al.
patent: 2003/0027207 (2003-02-01), Filpula
patent: 2003/0059911 (2003-03-01), Yamaoka et al.
patent: 2003/0100508 (2003-05-01), Simon et al.
patent: 2003/0190598 (2003-10-01), Tanha et al.
patent: 2004/0142379 (2004-07-01), St. Hilaire et al.
patent: 2005/0100963 (2005-05-01), Sato et al.
patent: 2005/0136428 (2005-06-01), Crea
patent: 2005/0245454 (2005-11-01), Goldstein
patent: 2005/0272093 (2005-12-01), MacKinnon
patent: 00436597 (1997-04-01), None
patent: WO 90/02809 (1990-03-01), None
patent: WO 95/34683 (1995-12-01), None
patent: WO 98/20036 (1998-05-01), None
patent: WO 98/20159 (1998-05-01), None
patent: WO 98/20169 (1998-05-01), None
patent: WO 99/29337 (1999-06-01), None
patent: WO 03/004604 (2003-01-01), None
patent: WO 03/011892 (2003-02-01), None
patent: WO 03/020201 (2003-03-01), None
Eng et al., 1990, Purification and Structure of Exendin-3, a New Pancreatic Secretagogue Isolated fromHeloderma horridumVenom, The Journal of Biological Chemistry, 265(33): 20259-20262.
Eng et al., 1992, Isolation and Characterization of Exendin-4, an Exendin-3 Analogue, fromHeloderma suspectumVenom, The Journal of Biological Chemistry, 267(11): 7402-7405.
Snow, C.D., et al., “The Trp Cage: Folding Kinetics and Unfolded State Topology via Molecular Dynamics Simulations,” Journal of the American Chemical Society, v. 124(49): 14548-14549, American Chemical Society, 2002.
Non-Final Office Action for US Patent No. 7,329,725, Mailed May 2, 2006 (8 pp.).
Final Office Action for US Patent No. 7,329,725, Mailed May 22, 2007, (22 pp.).
Examiner's Interview Summary for US Patent No. 7,329,725, Mailed Aug. 7, 2007 (3 pp.).
Examiner's Interview Summary for US Patent No. 7,329,725 Mailed Oct. 3, 2007; Interview Date Sep. 12, 2007 (2 pp.).
Agu, R.U., et al., “Intranasal Delivery of Recombinant Human Parathyroid Hormone [HPTH (1-34)], Teriparatide in Rats,” Endocrine Research, v. 30(3): pp. 455-467, Marcel Dekker, Inc., Aug. 2004.
Andersen, N.H., et al., “Optimizing Aqueous Fold Stability for Short Polypeptides: 20 Residue Miniprotein Constructs That Melt as High as at 61 degrees C,” Peptides: The Wave of the Future; Michal Lebl and Richard A. Houghten (Editors), p. 406, American Peptide Society, 2001.
Lane, N.E., “Parathyroid Hormone: Evolving Therapeutic Concepts 1,” Current Opinion Rheumatology, v. 16 (4) pp. 457-463, Jul. 2004.
Neidigh, J.W., et al., “Designing a 20-Residue Protein,” Nature Structural Biology; v. 9(6): pp. 425-430, Nature Publishing Group, Jun. 2002.
Desjobert, et al., “Identification By Phage Display Selection of a Short Peptide Able to Inhibit Only the Strand Transfer Reaction Catalyzed by Human Immunodeficiency Virus Type 1 Integrase,” Biochemistry, v. 43:pp. 13097-13105, American Chemical Society, 2004.
Fleming, et al., “Discovery of High-Affinity Peptide Binders to BLyS by Phage Display,” Journal of Molecular Recognition, v. 18: pp. 94-102, John Wiley & Sons, 2004.
Landon, et al., “Is Phage Display Technology on Target for Developing Peptide-Based Cancer Drugs?” Current Drug Discovery Technologies, v. 1: pp. 113-132, Bentham Science Publishers, 2004.
Molenaar, et al., “Uptake and Processing of Modified Bacteriophage M13 in Mice: Implications for Phage Display,” Virology, v. 293: pp. 182-191, Elsevier Science, 2002.
Kolonin, M.G., et al., “Reversal of Obesity by Targeted Ablation of Adipose Tissue,” Nature Medicine, v. 10: pp. 625-632, Nature Publishing Group, 2004.
Arap, W. et al., “Targeting the Prostrate for Destruction Through a Vascular Address,” v. 99(3): pp. 1527-1531, Proceedings of the National Academy of Sciences, 2002.
Maruta, F., et al., “Use of Phage Display Library to Identify Oligopeptides Binding to the Lumenal Surface of Polarized Endothelium by Ex Vivo Perfusion of Human Umbilical Veins,” Journal of Drug Targeting, v. 11(1): pp. 53-59, Informa Healthcare, 2003.
Samoylova, T.I. and Smith, B.F., “Elucidation of Muscle-Binding Peptides by Phage Display Screening,” Muscle Nerve, v. 22:460-466, John Wiley & Sons, 1999.
Nowakowski, G.S., et al., “A Specific Heptapeptide From a Phage Display Peptide Library Homes to Bone Marrow and Binds to Primitive Hematopoietic Stem Cells,” Stem Cells, v. 22: pp. 1030-1038, AlphaMed Press, 2004.
Jost, P.J., et al., “A Novel Peptide, THALWHT, for the Targeting of Human Airway Epithelia,” FEBS Letters, v. 489: pp. 263-269, Elsevier Science B.V., 2001.
Nicklin, S.A. et al., “Selective Targeting of Gene Transfer to Vascular Endothelial Cells by Use of Peptides Isolated by Phage Display,” Circulation, v. 102: pp. 231-237, American Heart Association, 2000.
Yip, Y.L., et al., “Biodistribution of Filamentous Phage-Fab in Nude Mice,” Journal of Immunological Methods, v. 225: pp. 171-178, Elsevier Science, 1999.
Dintilhac, A. and Bernues, J.; “HMGB1 Interacts With Many Apparently Unrelated Proteins by Recognizing Short Amino Acid Sequences” Journal of Biological Chemistry, v. 277(9): pp. 7021-7028, The American Society for Biochemistry and Molecular Biology, Inc., 2002.
Sankovich, S.E., et al., “Design and Assay of Inhibitors of HIV-1 Vpr Cell Killing and Growth Arrest Activity Using Microbial Assay Systems,” Journal of Biomolecular Screening, v. 3(4): pp. 299-304, The Society for Biomolecular Screening, 1998.
Work, L.M., et al., “Development of Efficient Viral Vectors Selective for Vascular Smooth Muscle Cells,” Molecular Therapy, v. 9(2): pp. 198-208, The American Society of Gene Therapy, 2004.
Menendez, A. and Scott, J.K., “The Nature of Target-Unrelated Peptides Recovered in the Screening of Phage Display Random Peptide Libraries with Antibodies,” Analytical Biochemistry, v. 336: pp. 145-157, Elsevier, 2004.
Baldwin et al., “Antitumor Monoclonal Antibodies for Radioimmunodetection of Tumors and Drug Targeting”, Cancer Metastasis Reviews, v. 2: pp. 89-106, Martinus Nijhoff Publishers, 1983.
Ponpipom, M.M., et al., “Cell-specific Ligands for Selective Drug Delivery to Tissues and Organs,” Journal of Medicinal Chemist
Badders Douglas L.
Herman Richard E.
Houston, Jr. Michael E.
Johnson Paul Hickok
Quay Steven C.
Bales Mark A.
Marina Biotech, Inc.
Marina Biotech, Inc.
Steele Amber D.
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