Wound care compositions

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

Reexamination Certificate

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C435S069400, C514S012200

Reexamination Certificate

active

07060795

ABSTRACT:
The invention provides polypeptides that can inhibit the activity of matrix metalloproteinases. Such polypeptides are useful for treating wounds, for example, chronic wounds.

REFERENCES:
patent: 5714465 (1998-02-01), Langley et al.
patent: 5914392 (1999-06-01), Hawkins et al.
patent: 1041083 (2000-10-01), None
Shimizu et al. Cloning and sequencing of the cDNA encoding a mouse tissue inhibitor of metalloproteinase-2. Gene. 1992. 114, 291-292.
Arnold, Ulrich, “Kinetic and Thermodynamic Thermal Stabilities of Ribonuclease A and Ribonuclease B”,Biochemistry, 36, (1997), 2166-2172.
Becker, Joseph W., “Stromelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme”,Protein Science, 4, (1995), 1966-1976.
Bodden, M. Kirby, et al., “Functional Domains of Human TIMP-1 (Tissue Inhibitor of Metalloproteinases)”,The Journal of Biological Chemistry, 269 (29), (1994), 18943-18952.
Browner, Michelle F., “Matrilysin-Inhibitor Complexes: Common Themes among Metalloproteases”,Biochemistry, 34, (1995), 6602-6610.
Butler, Georgina S., et al., “The Specificity of TIMP-2 for Matrix Metalloproteinases Can Be Modified by Single Amino Acid Mutations”,The Journal of Biological Chemistry, 274 (29), (1999), 20391-20396.
Colandrea, Teresa D., “Epidermal Expression of Collagenase Delays Wound-Healing in Transgenic Mice”,The Journal of Investigative Dermatology, (1998), 1029-1033.
Duivenvoorden, Wilhelmina C., “Use of Tetracycline as an Inhiitor of Matrix Metalloproteinase Activity Secreted by Human Bone-Metastasizing Cancer Cells”,Invasion Metastasis, 17, (1997), 312-322.
Fernandez-Catalan, Carlos, “Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor”,The EMBO Journal, 17 (17), (1998), 5238-5248.
Gabb, Henry A., et al., “Modelling Protein Docking using Shape Comlementarity, Electrostatics and Biochemical Information”,Journal of Molecular Biology, 272, (1997),1 06-120.
Gomis-Ruth, Franz-Xaver, “Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1”,Letters to Nature, 389, (1997), 77-81.
Grams, Frank, “X-ray structures of human neutrophil collagenase complexed with peptide hydrozamate and peptide thiol inhibitors”,European Journal of Biochemistry, 228, (1995), 830-841.
Guex, Nicolas, “Swiss-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling”,Electrophesis, 18, (1997), 2714-2723.
Higgins, Desmond G., “Clustal V: improved software for multiple sequence alignment”,Computer applications in the biosciences, 8 (2), (1992), 189-191.
Hodges, Deborah J., et al., “Preparation of recombinant tissue inhibitor of metalloproteinases-1 (TIMP-1) in high yield and identification of a hydrophobic surface feature”,Eur. J. Biochem, 257, (1998), 562-569.
Howard, Eric W., “Preferential Inhibition of 72- and 92-kDa Gelatinases by Tissue Inhibitor of Metalloproteinases-2”,The Journal of Biological Chemistry, 266 (20), (1991), 13070-13075.
Huang, Wen, “Folding and characterization of the amino-terminal domain of human tissue inhibitor of metalloproteinases-1 (TIMP-1) expressed at high yield inE. coli”,FEBS Letters, 384, (1996), 155-161.
Hutton, Mike, et al., “Analysis of the Interaction of TIMP-2 and MMPs: Engineering the Changes”,Annals of the New York Academy of Sciences, 878, (Jun. 1999), 524-527.
Kaiser, Donald A., et al., “Characterization of Actin and Poly-L-proline Binding Sites of Acanthamoeba Profilin with Monoclonal Antibodies and by Mutagenesis”,Journal of Molecular Biology, 256, (1996), 89-107.
Karlsson, Robert, et al., “Experimental Design for Kinetic Analysis of Protein-Protein Interactions with surface plasmon resonance biosensors”,Journal of Immunological Methods, 200, (1997), 121-133.
Levy, Daniel E., “Matrix Metalloproteinase Inhibitors: A Structure-Activity Study”,Journal of Medicinal Chemistry, 41, (1998), 199-223.
Libson, Andrew M., “Crystal structure of the haemopexin-like C-terminal domain of gelatinase A”,Nature Structural Biology, 2 (11), (1995), 938-942.
Liu, Yiliang E., et al., “Preparation and Characterization of Recombinant Tissue Inhibitor of Metalloproteinase 4 (TIMP-4)”,The Journal of Biological Chemistry, 272 (33), (1997), 20479-20483.
Lofas, Stefan, “Dextran modified gold for surfaces for surface plasmon resonance sesnors: immunoreactivity of immobilized antibodies and antibody-surface interaction studies”,Colloids and Surfaces B: Biointerfaces, 1, (1993), 83-89.
Meng, Qi, et al., “Residue 2 of TIMP-1 Is a Major Determinant of Affinity and Specificity for Matrix Metalloproteinases but Effects of Substitutions Do Not Correlate with Those of the Corresponding P1′ Residue of Sbustrate”,The Journal of Biological Chemistry, 274 (15), (1999), 10184-10189.
Morton, Thomas A., “Intetpreting Complex Binding Kinetics from Optical Biosensors: A Comparison of Analysis by Linearization, the Integrated Rate Equation, and Numerical Integration”,Analytical Biochemistry, 227, (1995), 176-185.
Moses, M. A., “Temporal Study of the Activity of Matrix Metalloproteinases and Their Endogenous Inhibitors During Wound Healing”,Journal of Cellular Biochemistry, 60, (1996), 379-386.
O'Shannessy, Daniel J., “Determination of Rate and Equilibrium Binding Constants for Macromolecular Interactions Using Surface Plasmon Resonance: Use of Nonlinear Squares Analysis Methods”,Analytical Biochemistry, 212, (1993), 457-468.
Odake, Shinjiro, “Inhibition of matrix metalloproteinase by peptidyl hydroxamic acids”,Biochemical and Biophysical Research Communications, 199 (3), (1994), 1442-1446.
Olson, Matthew W., “Kinetic Analysis of the Binding of Human Matrix Metalloproteinase-2 and -9 to Tissue Inhibitor of Metalloproteinase (TIMP)-1 and TIMP-2”,The Journal of Biological Chemistry, 272 (47), (1997), 29975-29983.
Overall, Christopher M., et al., “Identification of the Tissue Inhibitor of Metalloproteinases-2 (TIMP-2) Binding Site on the Hemopexin Carboxyl Domain of Human Gelatinase A by Sie-directed Mutagenesis”,The Journal of Biological Chemistry, 274 (7), (1999), 4421-4429.
Peitsch, Manuel C., “Automated Modelling of the Transmembrance Region of G-protein Coupled Receptor by Swiss-Model”,Receptors and Channels, 4, (1996), 161-164.
Peitsch, M. C., “ ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling”,Biochemical Society Transactions, 24, (1996), 274-279.
Quirk, Stephen, “Primary Structure of and Studies on Acanthamoeba Actophorin”,Biochemistry, 32(33), (1993), 8525-8533.
Reinemer, Peter, “Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases”,FEBS Letters, 338, (1994), 227-233.
Saarialho-Kere, U.K., “Patterns of matrix metaloproteinase and TMP expression in chronic ulcers”,Archives of Dermatological Research, 290, (1998), S47-S54.
Sanger, F., “DNA sequencing with chain-terminating inhibitors”,Proceedings of the National Academy of Sciences USA, 74 (12), (Dec. 1977), 5463-5467.
Sayle, Roger A., “RASMOL: biomolecular graphics for all”,Trends in Biochemical Sciences, 20, (1995), 333-379.
Siegel, Lewis M., “Determination of Molecular Weights and Frictional Ratios of Proteins . . . ”,Biochemica Et Biophysica Acta, 112, (1966), 346-362.
Su, Jui-Lan, “Monoclonal Antibodies against Human Collagenase and Stromelysin”,Hybridoma, 14 (4), (1995), 383-390.
Taylor, Kenneth B., “The Mechanism of Inhabitation of Collagenase by TIMP-1”,The Journal of Biological Chemistry, 271 (39

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