Methods for protein refolding

Details Methods for protein refolding Methods for protein refolding

2010-04-19

2011-11-29

Nashed, Nashaat (Department: 1656)

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Recombinant dna technique included in method of making a...

C435S183000, C530S402000

Reexamination Certificate

active

08067201

ABSTRACT:
Provided herein are methods for refolding proteins. The methods involve covalently modifying a denatured protein with a nonproteinaceous polymer and then renaturing the modified protein.

REFERENCES:
patent: 4179337 (1979-12-01), Davis et al.
patent: 4301144 (1981-11-01), Iwashita et al.
patent: 4496689 (1985-01-01), Mitra
patent: 4640835 (1987-02-01), Shimizu et al.
patent: 4670417 (1987-06-01), Iwasaki et al.
patent: 4791192 (1988-12-01), Nakagawa et al.
patent: 5235041 (1993-08-01), Cappello et al.
patent: 5766897 (1998-06-01), Braxton
patent: 5792742 (1998-08-01), Gold et al.
patent: 5932462 (1999-08-01), Harris et al.
patent: 6207446 (2001-03-01), Szostak et al.
patent: 6462189 (2002-10-01), Koide
patent: 6610281 (2003-08-01), Harris
patent: 6818418 (2004-11-01), Lipovsek et al.
patent: 7115396 (2006-10-01), Lipovsek et al.
patent: 7847062 (2010-12-01), Chen et al.
patent: 7858739 (2010-12-01), Chen et al.
patent: 2002/0019517 (2002-02-01), Koide
patent: 2002/0061307 (2002-05-01), Whitlow et al.
patent: 2003/0134352 (2003-07-01), Freimuth et al.
patent: 2003/0170753 (2003-09-01), Koide
patent: 2004/0142429 (2004-07-01), Grant et al.
patent: 2004/0146969 (2004-07-01), Furutani et al.
patent: 2005/0255548 (2005-11-01), Lipovsek et al.
patent: 2007/0031955 (2007-02-01), Lee et al.
patent: 2008/0125580 (2008-05-01), Pizarro et al.
patent: 2009/0054628 (2009-02-01), St. John et al.
patent: 04-108827 (1992-04-01), None
patent: WO-98/31700 (1998-07-01), None
patent: WO-98/56915 (1998-12-01), None
patent: WO-00/34784 (2000-06-01), None
patent: WO-01/64942 (2001-09-01), None
patent: WO-02/04523 (2002-01-01), None
patent: WO-02/32925 (2002-04-01), None
patent: WO-2004/113394 (2004-12-01), None
patent: WO-2008/097497 (2008-08-01), None
patent: WO-2009/025806 (2009-02-01), None
patent: WO-2009/073115 (2009-06-01), None
patent: WO-2009/142773 (2009-11-01), None
patent: WO-2010/060095 (2010-05-01), None
Kim et al. In vitro refolding of PEGylated lipase. J. Biotechnol. 131 (2007) 177-179.
Abuchowski et al., Alteration of Immunological Properties of Bovine Serum Albumin by Covalent Attachement of Polyethylene Glycol,J. Biol. Chem., 252:3578-3581 (1977).
Abuchowski et al., Effect of Covalent Attachment of Polyethylene Glycol on Immunogenicity and Circulating Life of Bovine Liver Catalase,J. Biol. Chem., 252:3582-3586 (1977).
Baron et al. H NMR Assignment and Secondary Structure of the Cell Adhesion Type III Module of Fibronectin.Biochemistry, 31:2068-2073 (1992).
Batori et al., Exploring the Potential of the Monobody Scaffold: Effects of Loop Elongation on the Stability of a Fibronectin Type III Domain,Protein Eng., 15(12):1015-1020 (2002).
Caliceti, P., et al., “Pharmacokinetic and biodistribution properties of poly(ethylene glycol)—protein conjugates,”Advanced Drug Delivery Reviews, 55:1261-1277 (2003).
Campbell & Spitzfaden, Building Proteins with Fibronectin Type III Modules,Structure, 2(5):333-337 (1994).
J Choy et al., Efficacy of a Novel PEGylated Humanized Anti-TNF Fragment (CDP870) in Patients with Rheumatoid Arthritis: a Phase II Double-Blinded, Randomized, Dose-Escalating Trial.Rheumatology, 41:1133-1137 (2002).
Clarke et al., Folding and Stability of a Fibronectin Type III Domain of Human Tenascin.J. Mol. Biol., 270: 771-778 (1997).
Cleland et al., Polyethylene Glycol Enhanced Refolding of Bovine Carbonic Anhydrase B,The Journal of Biological Chemistry, 267(19):13327-13334 (1992).
Copie et al., Solution Structure and Dynamics of Linked Cell Attachment Modules of Mouse Fibronectin Containing the RGD and Synergy Regions: Comparison with the Human Fibronectin Crystal Structure.J. Mol. Biol. 277:663-682 (1998).
Dickinson et al., Crystal Structure of the Tenth Type III Cell Adhesion Module of Human Fibronectin.J. Mol. Biol. 236:1079-1092 (1994).
Dickinson et al., Crystals of the Cell-Binding Module of Fibronectin Obtained from a Series of Recombinant Fragments Differing in Length.J. Mol. Biol. 238:123-127 (1994).
Grant et al., Structural Requirements for Biological Activity of the Ninth and Tenth Fill Domains of Human Fibronectin.J. Biol. Chem. 272:6159-6166 (1997).
Hocking et al., A Novel Role for the Integrin-Binding III-10 Module in Fibronectin Matrix Assembly.J. Cell Biol. 133:431-444 (1996).
Koide et al., Stabilization of a Fibronectin Type III Domain by the Removal of Unfavorable Electrostatic Interactions on the Protein Surface,Biochemistry, 40(34):10326-10333 (2001).
Koide et al., The Fibronectin Type III Domain as a Scaffold for Novel Binding Proteins.J. Mol. Biol. 284:1141-1151 (1998).
Leahy et al., Structure of a Fibronectin Type III Domain from Tenascin Phased by MAD Analysis of the Selenomethionyl Protein.Science258:987-991 (1992).
Leahy et al., “2.0 A Crystal Structure of Four-Domain Segment of Human Fibronectin Encompassing the RGD Loop and Synergy Region,”Cell, 84:155-164 (1996).
Litvinovich and Ingham, Interactions Between Type III Domains in the 110 kDa Cell-Binding Fragment of Fibronectin.J. Mol. Biol. 248:611-626 (1995).
Lombardo et al., Conformational Flexibility and Crystallization of Tandemly Linked Type III Modules of Human Firbonectin.Prot. Sci. 5:1934-1938 (1996).
Main et al., The Three-Dimensional Structure of the Tenth Type III Module of Fibronectin: An Insight into RGD-Mediated Interactions.Cell71:671-678 (1992).
Matsushima et al. Modification ofE. coliAsparaginase with 2,4-BIS(O-Methoxypolyethylene Glycol)-6-Chloro-S-Triazine (Activated PEG2); Disappearance of Binding Ability Towards Anti-Serum and Retenttion of Enzymic Activity.Chemistry Letters, p. 773-776 (1990).
Parker et al., “Antibody mimics based on human fibronectin type three domain engineered for thermostability and high-affinity binding to vascular endothelial growth factor receptor two”,Protein Engineering, Design&Selection, 18(9):435-444 (2005).
Plaxco et al. A Comparison of the Folding Kinetics and Thermodynamics of Two Homologous Fibronectin Type III Modules.J. Mol. Biol. 270:763-770 (1997).
Plaxco et al. Rapid Refolding of a Proline-Rich All-Beta-Sheet Fibronectin Type III Module.PNAS93:10703-10706 (1996).
Potts and Campbell. Structure and Function of Fibronectin Modules.Matrix Biol. 15:313-320 (1996).
Richards, J., et al., “Engineered Fibronectin Type III Domain with a RGDWXE Sequence Binds with Enhanced Affinity and Specificity to Human ανβ3 Integrin,”J. Mol. Biol. Science Direct. 326:1475-1488 (2003).
Roberts and Szostak. RNA-Peptide Fusions for the In Vitro Selection of Peptides and Proteins.PNAS94:12297-12302 (1997).
Roberts et al., Chemistry for peptide and protein PEGylation,Advanced Drug Delivery Reviews, 54:459-476 (2002).
Roberts, R.W. Totally in vitro protein selection using mRNA-protein fusions and ribosome display. Current Opinion in Chemical Biology, Current Biology Ltd, London, GB, 3, 268-273 (1999), XP002180767 ISSN: 1367-5931.
Ryan et al., Advances in PEGylation of imprtant biotech molecules: delivery aspects,Expert Opin. Drug Deliv. 5(4):371-383 (2008).
Xu et al., Directed Evolution of High-Affinity Antibody Mimics Using mRNA Display,Chemistry&Biology, 9:933-942 (2002).
Yang et al., “Tailoring Structure-Function and Pharmacokinetic Properties of Single-Chain Fv Proteins by Site-Specific PEGylation”,Protein Engineering, 16(10):761-770 (2003).

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