Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...
Reexamination Certificate
2007-06-12
2007-06-12
Wessendorf, T. D. (Department: 1639)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving antigen-antibody binding, specific binding protein...
C435S006120, C435S005000, C435S004000, C435S091500, C435S091500, C530S331000, C530S330000, C530S324000, C530S325000
Reexamination Certificate
active
10823006
ABSTRACT:
The invention is directed to a model system for structure-activity relationship analysis of peptide or protein molecules involved in important biological processes. Provided by the invention are combinatorial peptide libraries comprising peptides with a novel “tryptophan zipper” scaffold (trpzip) that forms stable β-hairpin structure in solution. Methods of selecting and using such scaffold are provided herein, which are useful for mimicking native protein structures and interactions and designing therapeutic agents. Thus, the invention has profound utility for biological studies and drug development.
REFERENCES:
patent: 4833092 (1989-05-01), Geysen
patent: 5223409 (1993-06-01), Ladner et al.
patent: 5534615 (1996-07-01), Baker et al.
patent: 5627024 (1997-05-01), Maruyama et al.
patent: 5766905 (1998-06-01), Studier et al.
patent: 5821047 (1998-10-01), Garrard et al.
patent: 5824483 (1998-10-01), Houston, Jr. et al.
patent: 5830851 (1998-11-01), Wrighton et al.
patent: 5866341 (1999-02-01), Spinella et al.
patent: 5885780 (1999-03-01), Olivera et al.
patent: 6013458 (2000-01-01), Kahn et al.
patent: 6100377 (2000-08-01), Greene
patent: 6180343 (2001-01-01), Anderson et al.
patent: 6475806 (2002-11-01), Benjamin et al.
patent: 6482591 (2002-11-01), Lockhart et al.
patent: 6878804 (2005-04-01), Robinson et al.
patent: 2003/0036093 (2003-02-01), Floudas et al.
patent: WO 92/00091 (1992-01-01), None
patent: WO 94/03494 (1994-02-01), None
patent: WO 95/01800 (1995-01-01), None
patent: WO 95/34683 (1995-12-01), None
patent: WO 97/29185 (1997-08-01), None
patent: WO 98/49168 (1998-11-01), None
patent: WO 99/51625 (1999-10-01), None
patent: WO 00/20574 (2000-04-01), None
patent: WO 00/77194 (2000-12-01), None
patent: WO 01/91780 (2001-12-01), None
Alexander et al., “Thermodynamic Analysis of the Folding of the Streptococcal Protein G IgG-Binding Domains B1 and B2: Why Small Proteins Tend to have High Denaturation Temperatures”,Biochemistry, 31:3597-3603 (1992).
Allen et al., “Finding prospective partners in the library: the two-hybrid system and phage display find a match”,TIBS, 20:511-516 (1995).
Ball et al., “Conformational Constraints: Nonpeptide β-Turn Mimics,”Journal of Molecular Recognition, 3(2):55-64 (1990).
Barbas, “Recent advances in phage display”,Current Opinion in Biotechnology, 4:526-530 (1993).
Barthe et al., Synthesis and NMR solution structure of an α-helical hairpin stapled with two disulfide bridges,Protein Science, 133:942-955 (2000) (abstract only).
Bass et al., “Hormone Phage: An Enrichment Method for Variant Proteins with Altered Binding Properties”,Proteins: Structure, Function, and Genetics, 8(4):309-314 (1990).
Becktel and Schellman, “Protein Stability Curves”,Biopolymers, 26:1859-1877 (1987).
Biachi et al., “A Conformationally Homogeneous Combinatorial Peptide Library”,J. Mol. Biol., 247:154-160 (1995).
Bianchi et al., “High level expression and rational mutagenesis of a designed protein, the minibody. From an insoluble to a soluble molecule,”Journal of Molecular Biology, 236(2):649-659 (Feb. 18, 1994).
Blanco et al., “A short linear peptide that folds into a native stable B-hairpin in aqueous solution”,Structural Biology, 1(9):584-590 (Sep. 1994).
Blanco, F. et al., “NMR Evidence of a Short Linear Peptide That Folds into a β-Hairpin in Aqueous Solution,”J. Am. Chem. Soc., 115(13):5887-5888 (1993).
Bradbury and Cattaneo, “The use of phage display in neurobiology”,Trends in Neuroscience, 18:243-249 (1995).
Choo and Klug, “Designing DNA-binding proteins on the surface of filamentous phage”,Current Opinion in Biotechnology, 6:431-436 (1995).
Chothia, “Coiling of B-Pleated Sheets”,J. Mol. Biol., 163:107-117 (1983).
Chou, P. et al., “Empirical Predictions Of Protein Conformation,”Ann. Rev. Biochem., 47:251-276 (1978).
Chrismann et al., “The cystine knot of a squash-type protease inhibitor as a structural scaffold for Escherichia coli cell surface display of conformationally constrained peptides,”Protein Engineering, 12(9):797-806 (Sep. 1999).
Clackson and Wells, “In vitro selection from protein and peptide librairies”,Trends Biotechnol., 12:173-184 (1994).
Clackson et al., “Making antibody fragments using phage display libraries”,Nature, 352:624-628 (1991).
Cochran et al., “A Minimal Peptide Scaffold for B-Turn Display: Optimizing a Strand Position in Disulfide-Cyclized B-Hairpins”,J. Am. Chem. Soc., 123:625-632 (2001).
Cochran, A., “Antagonists of protein-protein interactions”,Chemistry and Biology, 7(4):R85-R94 (Apr. 2000).
Constantine, K. et al., “Structural and Dynamic Properties of a β-Hairpin-Forming Linear Peptide. I. Modeling Using Ensemble-Averaged Constraints,”J. Am. Chem. Soc., 117(44):10841-10854 (1995).
Cortese et al., “Identification of biologically active peptides using random libraries displayed on phage”,Current Opinion in Biotechnology, 6:73-80 (1995).
Cortese et al., “Selection of biologically active peptides by phage display of random peptide librairies”,Current Opinion in Biotechnology, 7:616-621 (1996).
Cunningham and Wells, “High-Resolution Epitope Mapping of hGH-Receptor Interactions by Alanine-Scanning Mutagenesis”,Science, 244:1081-1085 (1989).
Cwirla et al., “Peptide agonist of the thrombopoietin receptor as potent as the natural cytokine”,Science, 276(5319):1696-1699 (Jun. 13, 1997).
Cwirla et al., “Peptides on phage: a vast library of peptides for identifying ligands”,Proc. Natl. Acad. Sci. USA, 87(16):6378-6382 (1990).
de Alba, E. et al., “Conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution,”Folding&Design, 1(2):133-144 (Feb. 26, 1996).
de Alba, E. et al., “Cross-strand side-chain interactons versus turn conformation in β-hairpin,”Protein Science, 6:2548-2560 (1997).
de Alba, E. et al., “Interactions responsible for the pH dependence of the β-hairpin conformational population formed by a designed linear peptide,”Eur. J. Biochem, 233:283-292 (1995).
de Alba, E. et al., “Turn Residue Sequence Determines β-Hairpin Conformation In Designed Peptides,”J. Am. Chem. Soc., 119(1):175-183 (1997).
Domingo et al., “Synthesis of a mixture of cyclic peptides based on the Bowman-Birk reactive site loop to screen for serine inhibitors”,International Journal of Protein and Peptide Research, 46:79-87 (1995).
Dunn, I.S., “Phage display of proteins”,Current Opinion in Biotechnology, 7:547-553 (1996).
Efimov et al., “Bacteriophage T4 as a Surface Display Vector”,Virus Genes, 10(2):173-177 (1995).
Espinosa and Gellman, “A Designed B-Hairpin Containing a Natural Hydrophobic Cluster”,Agnew. Chem. Int. Ed., 39(13):2330-2333 (2000).
Fairbrother et al., “Novel Peptides Selected to Bind Vascular Endothelial Growth Factor Target the Receptor-Binding State”,Biochemistry, 37:17754-17764 (1998).
Falcomer et al., “Chain Reversals in Model Peptides: Studies of Cystine-Containing Cyclic Peptides. 3. Conformational Free Energies of Cyclization of Tetrapeptides of Sequence Ac-Cys-Pro-X-Cys-NHMe”,J. Am. Chem. Soc., 114:4036-4042 (1992).
Favre et al., “Structural Mimicry of Canonical Conformations in Antibody Hypervariable Loops Using Cyclic Peptides Containing a Heterochiral Diproline Template”,J. Am. Chem. Soc., 121:2679-2685 (1999).
Felioi, “Selection of antibody ligands from a large library of oligopeptides expressed on a multivalent exposition Vector”,J. Mol. Biol., 222:301-310 (1991).
Fowlkes et al., “Multipurpose Vectors for Peptide Expression on the M13 Viral Surface”,BioTechniques, 13(3):422-427 (19
Cochran Andrea G.
Skelton Nicholas
Starovasnik Melissa A.
Genentech Inc.
Merchant & Gould P.C.
Wessendorf T. D.
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