Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2002-12-17
2009-10-13
Robinson, Hope A (Department: 1652)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C514S012200, C514S017400, C530S350000, C530S300000
Reexamination Certificate
active
07601685
ABSTRACT:
Proteins are incorporated into protein or polysaccharide matrices for use in tissue repair, regeneration and/or remodeling and/or drug delivery. The proteins can be incorporated so that they are released by degradation of the matrix, by enzymatic action and/or diffusion. As demonstrated by the examples, one method is to bind heparin to the matrix by either covalent or non-covalent methods, to form a heparin-matrix. The heparin then non-covalently binds heparin-binding growth factors to the protein matrix. Alternatively, a fusion protein can be constructed which contains a crosslinking region such as a factor XIIIa substrate and the native protein sequence. Incorporation of degradable linkages between the matrix and the bioactive factors can be particularly useful when long-term drug delivery is desired, for example in the case of nerve regeneration, where it is desirable to vary the rate of drug release spatially as a function of regeneration, e.g. rapidly near the living tissue interface and more slowly farther into the injury zone. Additional benefits include the lower total drug dose within the delivery system, and spatial regulation of release which permits a greater percentage of the drug to be released at the time of greatest cellular activity.
REFERENCES:
patent: 4613665 (1986-09-01), Larm
patent: 4810784 (1989-03-01), Larm
patent: 5100668 (1992-03-01), Edelman et al.
patent: 5171670 (1992-12-01), Kronenberg et al.
patent: 5202247 (1993-04-01), Kilbum et al.
patent: 5428014 (1995-06-01), Labroo et al.
patent: 5504001 (1996-04-01), Foster
patent: 5561982 (1996-10-01), Tunkel et al.
patent: 5582862 (1996-12-01), Reed
patent: 5641670 (1997-06-01), Treco et al.
patent: 5693341 (1997-12-01), Schroeder et al.
patent: 5773577 (1998-06-01), Cappello
patent: 5840837 (1998-11-01), Krstenansky et al.
patent: 5877153 (1999-03-01), Harris et al.
patent: 5958874 (1999-09-01), Clark et al.
patent: 6117425 (2000-09-01), MacPhee et al.
patent: 6136564 (2000-10-01), Kopetzki et al.
patent: 6197325 (2001-03-01), MacPhee et al.
patent: 6331422 (2001-12-01), Hubbell
patent: 6468543 (2002-10-01), Gilbertson
patent: 6559119 (2003-05-01), Burgess et al.
patent: 7247609 (2007-07-01), Lutolf et al.
patent: 200 10 297 (2000-08-01), None
patent: WO 89/00051 (1989-01-01), None
patent: WO 90/05177 (1990-05-01), None
patent: WO 92/02620 (1992-02-01), None
patent: WO 92/09301 (1992-06-01), None
patent: WO 92/22312 (1992-12-01), None
patent: WO 94/20133 (1994-09-01), None
patent: WO 95/05396 (1995-02-01), None
patent: WO 95/23611 (1995-09-01), None
patent: WO 96/17633 (1996-06-01), None
patent: WO 97/24445 (1997-07-01), None
patent: WO 99/31137 (1999-06-01), None
patent: WO 00/64481 (2000-11-01), None
patent: WO 01/76558 (2001-10-01), None
patent: WO 03/040235 (2003-05-01), None
Borth (JBC, vol. 266, No. 27, Sep. 1991, pp. 181149-18153).
Hettasch et al. (JBC, vol. 272, No. 40, Oct. 1997, pp. 25149-25156).
Kahlem et al., PNAS, 1996, vol. 93, pp. 14580-14585.
Gupta et al. (J. Vas. Res., vol. 44, No. 5, 2007, faxed pp. 1-12).
Besson, et al., “Synthetic peptide substrates for a conductimetric assay ofPseudomonas aeruginosaelastase,”Analytical Biochemistry237(0232):216-223 (1996).
Borrajo, et al., “Derivatized Cyclodextrins as peptidometics: Influence on Neurite Growth,”Bioorganic and Medicinal Chemistry Letters7:1185-90 (1997).
Coombs, et al. “Directing sequence-specific proteolysis to new targets. The influence of loop size and target sequence on selective proteolysis by tissue-type plasminogen activator and urokinase-type plasminogen activator,”J. Biol. Chem.273(8):4323-8 (1998).
Dimilla, et al., “Mathematical model for the effects of adhesion and mechanics on cell migration speed,”Biophys. J.60(1):15-37 (1991).
Dinbergs, et al., “Cellular response to transforming growth factor-beta1 and basic fibroblast growth factor depends on release kinetics and extracellular matrix interactions,”J. Biol. Chem.271(47):29822-9 (1996).
Edelman, et al., “Basic fibroblast growth factor enhances the coupling of intimal hyperplasia and proliferation of vasa vasorum in injured rat arteries,”J. Clin. Invest.89(2):465-73 (1992).
Edelman, et al., “Controlled and modulated release of basic fibroblast growth factor,”Biomaterials.12(7):619-26 (1991).
Edelman, et al., “Perivascular and intravenous administration of basic fibroblast growth factor: vascular and solid organ deposition,”Proc. Natl. Acad. Sci. U. S. A.90(4):1513-7 (1993).
Edgar, et al., “The heparin-binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival,”EMBO J.3(7)1463-8 (1984).
Gotz, et al., “Neurotrophin-6 is a new member of the nerve growth factor family,”Nature372(6503):266-9 (1994).
Grainger, et al., “Poly(dimethylsiloxane)-poly(ethylene oxide)-heparin block copolymers. I. Synthesis and Characterization,”J. Biomed Mater Res.22(3): 231-249 (1988).
Harada, et al., “Basic fibroblast growth factor improves myocardial function in chronically ischemic porcine hearts,”J. Clin. Invest.94(2):623-30 (1994).
Hata, et al., “Binding of lipoprotein lipase to heparin. Identification of five critical residues in two distinct segments of the amino-terminal domain,”J. Biol. Chem.268(12):8447-57 (1993).
Haugen, et al, “Central and peripheral neurite outgrowth differs in preference for heparin-binding versus Integrin-binding sequences,”J. Neurosci.12(6):2034-42 (1992).
Herbert, et al., “Effects of fibinolysis on neurite growth from dorsal root ganglia cultured in two- and three-dimensional fibrin gels,”J. Comp. Neurol.365(3):380-91 (1996).
Herbert, et al., “Effects of fibrin micromorphology on neurite growth from dorsal root ganglia cultured in three-dimensional fibrin gels,”J. Biomed. Mat. Res.40(4)551-9 (1998).
Kallapur, et al, “The neural cell adhesion molecule (NCAM) heparin binding domain binds to cell surface heparan sulfate proteoglycans,”J. Neuro. Res.33(4):538-48 (1992).
Kaneda, et al., “Midkine, a heparin-binding growth/differentiation factor, exhibits nerve cell adhesion and guidance activity for neurite outgrowth in vitro,”J. Biochem.119(6)1150-6 (1996).
Kiguchi, et al., “Altered expression of epidermal growth factor receptor ligands in tumor promoter-treated mouse epidermis and in primary mouse skin tumors induced by an initiation-promotion protocol,”Mol. Carcinog.22(2):73-83 (1998).
Kinosaki, et al., “Identification of heparin-binding stretches of a naturally occurring deleted variant of hepatocyte growth factor (dHGF),”Biochim. Biophys. Acta.1384(1):93-102 (1998).
Kleinman, et al., “The laminins: a family of basement membrane glycoproteins important in cell differentiation and tumor metastases,”Vitam. Horm.47:161-86 (1993).
Lopez, et al., “Basic fibroblast growth factor in a porcine model of chronic myocardial ischemia: a comparison of angiographic, echocardiographic and coronary flow parameters,”J. Pharmacol Exp. Ther.282(1):385-90 (1997).
Lopez, et al., “Local perivascular administration of basic fibroblast growth factor: drug delivery and toxicological evaluation,”Drug Metab. Dispos.24(8):922-4 (1996).
Martin & Timpl, “Laminin and other basement membrane components,”Annu. Rev. Cell. Biol.3:57-85 (1987).
Massia, et al., “An RGD spacing of 440 nm is sufficient for integrin alpha V beta 3-mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation,”J. Cell. Biol.114(5):1089-100 (1991).
McCaffrey, et al., “Transforming growth factor-beta 1 is a heparin-binding protein: identification of putative heparin-binding regions and isolation of heparins with varying affinity for TGF-beta 1,”J. Cell. Physiol.152(2):430-40 (1992).
Netzel-Arnett, et al., “Sequence specificities of human fibroblast and neutrophil collagenases,”J. Biol.
Hubbell Jeffrey A.
Sakiyama-Elbert Shelly E.
Schense Jason C.
Eidgenossische Technische Hochschule Zurich
Pabst Patent Group LLP
Robinson Hope A
Universitat Zurich
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