Polyalkylene oxide-modified single chain polypeptides

Details Polyalkylene oxide-modified single chain polypeptides Polyalkylene oxide-modified single chain polypeptides

2004-08-02

2009-12-15

Steele, Amber D. (Department: 1639)

Drug, bio-affecting and body treating compositions

Conjugate or complex of monoclonal or polyclonal antibody,...

C530S391100, C530S387100

Reexamination Certificate

active

07632504

ABSTRACT:
The present invention relates to the chemical modification of single chain polypeptides by means of covalent attachment of strands of poly(ethylene glycol) PEG and similar poly(alkylene oxides) to single chain polypeptide binding molecules that have the three dimensional folding and, thus, the binding ability and specificity, of the variable region of an antibody. Such preparations of modified single chain polypeptide binding molecules have reduced immugenicity and antigenicity as well as having a longer halflife in the bloodstream as compared to the parent polypeptide. These beneficial properties of the modified single chain polypeptide binding molecules make them very useful in a variety of therapeutic applications. The invention also relates to multivalent antigen-binding molecules capable of PEGylation. Compositions of, genetic constructions for, methods of use, and methods for producing PEGylated antigen-binding proteins are disclosed.

REFERENCES:
patent: 4179337 (1979-12-01), Davis et al.
patent: 4704692 (1987-11-01), Ladner
patent: 4881175 (1989-11-01), Ladner
patent: 4904582 (1990-02-01), Tullis
patent: 4946778 (1990-08-01), Ladner et al.
patent: 5049504 (1991-09-01), Maugh et al.
patent: 5091513 (1992-02-01), Huston et al.
patent: 5122614 (1992-06-01), Zalipsky
patent: 5166320 (1992-11-01), Wu et al.
patent: 5202236 (1993-04-01), Maugh et al.
patent: 5202256 (1993-04-01), Maugh et al.
patent: 5212075 (1993-05-01), Bednarski et al.
patent: 5258498 (1993-11-01), Huston et al.
patent: 5260203 (1993-11-01), Ladner et al.
patent: 5438040 (1995-08-01), Ekwuribe
patent: 5443953 (1995-08-01), Hansen et al.
patent: 5455030 (1995-10-01), Ladner et al.
patent: 5482858 (1996-01-01), Huston et al.
patent: 5518889 (1996-05-01), Ladher et al.
patent: 5521291 (1996-05-01), Curiel et al.
patent: 5534254 (1996-07-01), Huston et al.
patent: 5534621 (1996-07-01), Ladner et al.
patent: 5547932 (1996-08-01), Curiel et al.
patent: 5635603 (1997-06-01), Hansen et al.
patent: 5656465 (1997-08-01), Panicali et al.
patent: 5661025 (1997-08-01), Szoka, Jr. et al.
patent: 5714350 (1998-02-01), Co et al.
patent: 5730990 (1998-03-01), Greenwald et al.
patent: 5753204 (1998-05-01), Huston et al.
patent: 5763733 (1998-06-01), Whitlow et al.
patent: 5766897 (1998-06-01), Braxton
patent: 5767260 (1998-06-01), Whitlow et al.
patent: 5844107 (1998-12-01), Hanson et al.
patent: 5853723 (1998-12-01), Jacobs et al.
patent: 5856456 (1999-01-01), Whitlow et al.
patent: 5869620 (1999-02-01), Whitlow et al.
patent: 5872222 (1999-02-01), Chang
patent: 5888773 (1999-03-01), Jost et al.
patent: 5981273 (1999-11-01), Curiel et al.
patent: 5990275 (1999-11-01), Whitlow et al.
patent: 5998144 (1999-12-01), Reff et al.
patent: 6022735 (2000-02-01), Curiel et al.
patent: 6025158 (2000-02-01), Gonzalez et al.
patent: 6027725 (2000-02-01), Whitlow et al.
patent: 6077663 (2000-06-01), Curiel et al.
patent: 6117980 (2000-09-01), Gonzalez et al.
patent: 6258562 (2001-07-01), Salfeld et al.
patent: 6323322 (2001-11-01), Filpula et al.
patent: 6515110 (2003-02-01), Whitlow et al.
patent: 6787153 (2004-09-01), Hosokawa et al.
patent: WO91/19739 (1991-12-01), None
patent: WO9119739 (1991-12-01), None
patent: WO 92/16555 (1992-10-01), None
patent: WO 93/11161 (1993-06-01), None
patent: WO 94/04691 (1994-03-01), None
patent: WO 94/12520 (1994-06-01), None
patent: WO 95/11020 (1995-04-01), None
patent: WO 96/09325 (1996-03-01), None
patent: WO9609325 (1996-03-01), None
patent: WO 96/13599 (1996-05-01), None
patent: WO 96/23794 (1996-08-01), None
patent: WO 96/40731 (1996-12-01), None
patent: WO 97/14719 (1997-04-01), None
patent: WO 98/25971 (1998-06-01), None
patent: WO 99/64460 (1999-12-01), None
Abuchowski, A. et al., “Alteration of Immnological Properties of Bovine Serum Albumin by Covalent Attachment of Polyethylene Glycol,”J. Biol. Chem. 252:3578-3581, The American Society of Biological Chemists, Inc. (1977).
Abuchowski, A. and F.F. Davis, “Soluble Polymer-Enzyme Adducts,” in: Enzymes as Drugs, Holcenberg, J.S. and J. Roberts, eds., John Wiley & Sons, Inc., New York, NY, pp. 367-383 (1981).
Abuchowski, A. et al., “Cancer Therapy with Chemically Modified Enzymes. I. Antitumor Properties of Polyethylene Glycol-Asparaginase Conjugates,” CancerBIochem Biophys7:175-186, Gordon and Breach Science Publishers, Inc. (1984).
Amit, A.G. et al., Three Dimensional Structure of an Antigen-Antibody Complex at 2.8 A Resolution,Science223:747-753, Association for the Advancement of Science (1986).
Anand, N. N. et al., Bacterial Expression and Secretion of Various Single-chain Fv Genes Encoding Proteins Specific for aSalmonellaSerotype B O-Antigen,,,J. Biol. Chem. 266:21874-21879, The American Society for Biochemistry and Molecular Biology, Inc. (1991).
Avrameas, A. et al., Polyreactive anti-DNA monoclonal antibodies and a derived peptide as vectors for the intracytoplasmic and intranuclear translocation of macromolecules,Proc. Natl. Acad. Sci. USA95:5601-5606 (May 1998).
Beauchamp, C.O. et al., “A New Procedure for the Synthesis of Polyethylene Glycol-Protein Adducts; Effects on Function, Receptor Recognition, and Clearance of Superoxide Dismutase, Lactoferrin, and α2-Macroglobulin,”Analytical Biochem. 131:25-33, Academic Press, Inc. (1983).
Benhar, I. et al., “Mutations of Two Lysine Residues in the CDR Loops of a Recombinant Immunotoxin That Reduce Its Sensitivity to Chemical Derivatization,”Bioconj. Chem5:321-326, American Chemical Society (1994).
Bird, R.E. et al., “Single-Chain Antigen-Binding Proteins,”Science 242:423-426, Association for the Advancement of Science (1988).
Bogdanov Jr., A., et al., “Graft Copolymers as Carriers for Systemic Delivery of Expression Vectors,”Proceed. Intl. Symp. Control. Rel. Bioact. Mater. 25:91-92, (Jun. 1998).
Chen, S.-Y. et al., “Design of a Genetic Immunotoxin to Eliminate Toxin Immunogenicity,”Gene Ther2:116-123, Stockton Press (1995).
Co, M.S. et al., “Chimeric and Humanized Antibodies with Specificity for the CD33 Antigen,” J.Immunol., 148:1149-1154, The American Association of Immunologists (1992).
Colcher, D. et al., “In Vivo Tumor Targeting of a Recombinant Single-Chain Antigen-Binding Protein,” J.Nat'l. Cancer Inst. 82:1191-1197 (1990).
Cumber, A.J. et al., “Comparative Stabilities In Vitro and In Vivo of a Recombinant Mouse Antibody FvCys Fragment and A bis Fv Cys Conjugate,”J. Immunol. 149:120-126, The American Association. Of lmmunologists (1992).
Delente, J.J., “Glycosylation revisited,”Trends in Biotechnol. 3:218, Elsevier Science Publishers B.V. (1985).
Desplancq, D. et al., “Multimerization Behaviour of Single Chain Fv Variants for the Tumor-Binding Antibody B72.3,”Protein Engineeringvol. 7 No. 8 pp. 1027-1033 (1994).
Eldin, P. et al., “High-Level Secretion of Two Antibody Single Chain Fv Fragments byPichia Pastoris,” J. Immunol. Methods 201 (1997) 67-75.
Filpula, D. et al., “Pegylated sFV and Glycosylated sFV,” Antibody Engineering Dec. 3-5, 1997.
Filpula, D. et al., “Pegylated sFV and Glycosylated sFV,” Antibody Engineering Dec. 3-5, 1997.
Filpula, D. et al., “Production of Single-Chain Fv Monomers and Multimers,” Antibody Engineering A Practical Approach.
Fominaya, J. et al., “Target Cell-Specific DNA Transfer Mediated by a Chimeric Multidomain Protein,”J. Biol. Chem. vol. 271, No. 18, Issue of May 8, pp. 10560-10568, (1996).
Gavel, Y. et al., “Sequence Differences Between Glycosylated and Non-Glycosylated Asn-X-Thr/Ser Acceptor Sites: Implications for Protein Engineering,”.
George, T. et al., “Production of a Bispecific Antibody by Linkage of Two Recombinant Single Chain Fv Molecules,”J. Cellular BiochemistrySupplement 15E, Mar. 8, 1991-Mar. 26, 1991.
Goodson, R. J. et al., “Site-Directed Pegylation of Recombinant Interleukin-2 at its Glycosylation Site”J. Cellular BiochemistryBio/T

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