Polyalkylene oxide-modified single chain polypeptides

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

2005-03-29

2005-03-29

Celsa, Bennett (Department: 1639)

Drug, bio-affecting and body treating compositions

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

C530S391100

Reexamination Certificate

active

06872393

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), Ladner et al.
patent: 5521291 (1996-05-01), Curiel et al.
patent: 5534254 (1996-07-01), Huston 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: 5753204 (1998-05-01), Huston et al.
patent: 5844107 (1998-12-01), Hanson et al.
patent: 5853723 (1998-12-01), Jacobs 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: WO 9216555 (1992-10-01), None
patent: WO 9311161 (1993-06-01), None
patent: WO 9404691 (1994-03-01), None
patent: WO 9412520 (1994-06-01), None
patent: WO 9511020 (1995-04-01), None
patent: WO 9609325 (1996-03-01), None
patent: WO 9613599 (1996-05-01), None
patent: WO 9623794 (1996-08-01), None
patent: WO 9640731 (1996-12-01), None
patent: WO 9714719 (1997-04-01), None
patent: WO 9825971 (1998-06-01), None
patent: WO 9964460 (1999-12-01), None
Abuchowski, A. et al., “Alteration of Immunological 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,”Cancer Biochem. Biophys. 7:175-186, Gordon and Breach Science Publishers, Inc. (1984).
Amit, A.G et al., “Three Dimensional Structure of an Antigen-Antibody Complex at 2.8 Å Resolution,”Science 233:747-753, 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 a Salmonella Serotype 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. USA 95:5601-5606, The National Academy of Sciences of the USA (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. Chem. 5:321-326, 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, The Controlled Release Society, Inc. (Jun. 1998).
Chen, S.-Y. et al., “Design of a genetic immunotoxin to eliminate toxin immunogenicity,”Gene Ther. 2:2:116-123, 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. Natl. Cancer Inst. 82:1191-1197, The National Cancer Institute (1990).
Cumber, A.J. et al., “Comparative Stabilities in Vitro and In Vivo of a Recombinant Mouse Antibody FvCys Fragment and A bisFvCys Conjugate,”J. Immunol. 149:120-126, The American Association of Immunologists (1992).
Delente, J.J., “Glycosylation revisited,”Trends in Biotechnol. 3:218, Elsevier Science Publishers B.V. (1985).
Desplancq, D. et al., “Multimerization behavior of single chain Fv variants for the tumour-binding antibody B72.3,”Protein Engineering 7:1027-1933, Oxford University Press (1994).
Eldin, P. et al., “High-level secretion of two antibody single chain Fv fragments byPichia pastoris,” J. Immunol. Meth. 201:67-75, Elsevier Science B.V. (Feb. 1997).
Filpula, D. et al., “Production of single-chain Fv monomers and multimers,” inAntibody Engineering: A Practical Approach,McCafferty, J., et al., eds., IRL Press, (Oxford University Press), Oxford, UK, pp. 253-268 (Aug. 1996).
Filpula, D., “PEGylated sFv and Glycosylated sFv,” Slide Presentation at: IBC's Eighth Annual International Conference on Antibody Engineering: New Technology, Application & Commercialization, Dec. 3, 1997.
Filpula, D., “PEGylated sFv and Glycosylated sFv,” Abstract from: IBC's Eighth Annual International Conference on Antibody Engineering: New Technology, Application & Commercialization, meeting date Dec. 3, 1997.
Fominaya, J. and W. Wels, “Target Cell-specific DNA Transfer Mediated by a Chimeric Multidomain Protein,”J. Biol. Chem. 271:10560-10568, The American Society for Biochemistry and Molecular Biology, Inc. (May 1996).
Gavel, Y., and G. von Heijne, “Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering,”Protein Engineering 3:433-442, Oxford University Press (1990).
George, A.J.T. et al., “Production of a Bispecific Antibody by Linkage of Two Recombinant Single Chain Fv Molecules,”J. Cell. Biochem. Suppl. 15E:127, Abstract No. N 206, Wiley-Liss (1991).
Goodson, R.J. and N.V. Katre, “

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