Fusion peptides isolatable by phase transition

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

Reexamination Certificate

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C530S412000, C530S387300, C530S351000, C530S303000, C530S307000, C530S306000, C530S308000, C530S311000, C530S399000, C530S302000, C530S301000, C435S189000, C435S229000, C435S227000, C435S213000, C435S226000, C435S183000

Reexamination Certificate

active

06852834

ABSTRACT:
Genetically-encodable, environmentally-responsive fusion proteins comprising ELP peptides. Such fusion proteins exhibit unique physico-chemical and functional properties that can be modulated as a function of solution environment. The invention also provides methods for purifying the FPs, which take advantage of these unique properties, including high-throughput purification methods that produce high yields (e.g., milligram levels) of purified proteins, thereby yielding sufficient purified product for multiple assays and analyses. The high throughput purification technique is simpler and less expensive than current commercial high throughput purification methods, since it requires only one transfer of purification intermediates to a new multiwell plate.

REFERENCES:
patent: 4783523 (1988-11-01), Urry et al.
patent: 4870055 (1989-09-01), Urry et al.
patent: 4898926 (1990-02-01), Urry
patent: 5028419 (1991-07-01), Pigiet
patent: 5235041 (1993-08-01), Cappello et al.
patent: 5243038 (1993-09-01), Ferrari et al.
patent: 5496712 (1996-03-01), Cappello et al.
patent: 5514581 (1996-05-01), Ferrari et al.
patent: 5527610 (1996-06-01), Urry
patent: 5641648 (1997-06-01), Ferrari et al.
patent: 5646016 (1997-07-01), McCoy et al.
patent: 5770697 (1998-06-01), Ferrari et al.
patent: 5773249 (1998-06-01), Cappello et al.
patent: 5792506 (1998-08-01), Buchanan et al.
patent: 5830713 (1998-11-01), Ferrari et al.
patent: 5854387 (1998-12-01), Urry et al.
patent: 5900405 (1999-05-01), Urry
patent: 5919657 (1999-07-01), Hillman et al.
patent: 5952034 (1999-09-01), Buchanan et al.
patent: 5972406 (1999-10-01), Urry et al.
patent: 5985261 (1999-11-01), White et al.
patent: 6004782 (1999-12-01), Daniell et al.
patent: 6013857 (2000-01-01), Deboer et al.
patent: 6018030 (2000-01-01), Ferrari et al.
patent: 6140072 (2000-10-01), Ferrari et al.
patent: 6184348 (2001-02-01), Ferrari et al.
patent: 6328996 (2001-12-01), Urry
patent: 6355776 (2002-03-01), Ferrari et al.
patent: WO9632406 (1996-10-01), None
Urry, D.W., et al., Phase-structure Transitions of the Elastin Polypentapeptide-water system within the framework of composition-temperature studies,Biopolymers, 24:2345-2346, (1985).
Porath, J. et al., Immobilized metal ion affinity chromatography,Prot. Expr. Purif., 3:262-282 (1992).
Homgren, A., Thioredoxin,Annu. Rev. Biochem, 54:237-271 (1985).
Smith, P.K., et al., Measurement of protein using bicinchonic acid,Anal. Biochem, 150:76-85 (1986).
Holmgren, A. et al., Enzymatic reduction-oxidation of protein disulfides by thioredoxin,Methods Enzymol, 107:295-300 (1984).
Meyer, D. and Chilkoti, Purification of Recombinant Proteins by Fusion with Thermally Responsive Polypeptides,Nat. Biotechnol, 17:1112-1115 (1999).
McPherson, D., et al., Production and purification of a recombinant elastomeric polypeptide, G-(VPGVG)19-VPGV fromEschericia coli, Biotechnol, Prog., 8:347-352 (1992).
Urry, D.W., Entropic Elastic Processes in Protein Mechanisms. I. Elastic Structure Due to an Inverse Temperature Transition and Elasticity Due to Internal Chain Dynamics,Journal of Protein Chemistry, vol. 7, No. 1, pp. 1-34 (1988).
Urry, D.W., Free Energy Transduction in Polypeptides and Proteins Based on Inverse Temperature Transitions,Prog. Biophys. Molec. Biol., vol. 57, pp. 23-57, (1992).
Urry, D.W., Physical Chemistry of Biological Free Energy Transduction as Demonstrated by Elastic Protein-Based Polymers,J. Phys. Chem. B, vol. 101, No. 51, pp. 11007-11028, (1997).
McPherson, et al., Product Purification by Reversible Phase Transition FollowingEscherichia coliExpression of Genes Encoding up to 251 Repeats of the Elastomeric Pentapeptide GVGVP,Protein Expression and Purification, 7, pp. 51-57, (1996).
Hoffman, A.S., Applications of Thermally Reversible Polymers and Hydrogels in Therapeutics and Diagnostics,Journal of Controlled Release, 6, pp. 297-305, (1987).
Chen, J.P., et al., Polymer-protein conjugates, II. Affinity precipitation separation of human immunogammaglobulin by a poly(N-isopropylacrylamide)-protein A conjugate,Biomaterials, 11:631-634 (1990).
Chilkoti, A., et al., Site-Specific Conjugation of a Temperature-Sensitive Polymer to a Genetically-Engineered Protein,Bioconjugate Chemistry, vol. 5, pp. 504-507, (1994).
Nilsson, B., et al., Fusion proteins in biotechnology and structural biology,Curr. Ipin. Struct. Biol., 2:569-575 (1992).
Uhlen, M. and Moks, Tomas, Gene Fusions for Purpose of Expression: An Introduction,Methods of Enzymology, vol. 185, pp. 129-143 (1990).
Maina, C.V., et al., AnEschericia colivector to express and purify foreign proteins by fusion to and separation from maltose-binding protein,Gene, 74:365-373 (1988).
Smith, D.B., et al., Single-step purification of polypeptides expressed inEscherichia colias fusions with glutathione S-transferase,Gene, 67:31-40 (1988).
Tsao, Kwe-Lan, et al., A versatile plasmid expression vector for the production of biotinylated proteins by site-specific, enzymatic modification inEscherichia coli, Gene, 169:59-64 (1996).
Smith, P.A., et al., A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins inEscherichia coli, Nucleic Acids Research, vol. 26, No. 6 (1998).
LaVallie, E.R., et al., A Thioredoxin Gene Fusion Expression System That Circumvents Inclusion Body Formation in theE. coliCytoplasm,Bio/Technology, vol. 11, pp. 187-193 (1993).
Ong, E. et al., The cellulose-binding domains of cellulases: tools for biotechnology,Trends. Biotechnol., 7:239-243 (1989).
Smith, Michele C. et al., Chelating Peptide-immobilized Metal Ion Affinity Chromatography,The Journal of Biological Chemistry, vol. 263, No. 15, pp. 7211-7215, (1988).
Kim, Jin-Soo et al., Ribonuclease S-peptide as a carrier in fusion proteins,Protein Science, 2:348-356, (1993).
Su, Xinzhuan, et al., production ffo Recombinant Porcine IumorNecrosis Factor Alpha in a NovelE. coliExpression System,Biotechniques, 13:756-765 (1992).
Nilsson, J. et al., Affinity Fusion Strategies for Detection, Purification, and Immobilization of Recombinant Proteins,Protein Expression and Purification, 11:1-16 (1997).
Hauck, M. L. et al., Local Hyperthermia Improves Uptake of a Chimeric Monoclonal Antibody in a Subcutaneous Xenograft Model,Clin. Cancer Res., 3:63-70 (1997).
Cope, D.A. et al., Enhanced Delivery of a Monoclonal Antibody F(ab1)2Fragment to Subcutaneous Human Glioma Xenografts Using Local Hyperthermia,Cancer Res., 50:1803-1809, (1990).
Vertesy, L. et al., Tendamistat (HOE 467), a tight-binding α-amylase inhibitor fromStreptomyces tendae4158,Eur. J. Biochem, 141:505-512, (1984).
Urry, D.W., et al., Temperature of Polypeptide Inverse Temperature Transition Depends on Mean Residue Hydrophobicity,J. Am. Chem. Soc., 113:4346-4348, (1991).
Kobatake, Eiry, et al., “Design and Gene Engineering Synthesis of an Extremely Thermostable Protein with Biological Activity,” Biomacromolecules 2000, 1: 382-386.
Meyer, Dan E., et al., “Protein Purificaiton by Fusion with an Environmentally Responsive Elastin-Like Polypeptide: Effect of Polypeptide Length on the Purification of Thioredoxin,” Biotechnol. Prog. 2001, 17 (4): 720-728.
Meyer, Dan E., et al. “Targeting a Genetically Engineered Elastin-like Polypeptide to Solid Tumors by Local Hypothermia,” Cancer Res Feb. 15, 2000; 61(4): 1548-54.
Meyer, Dan E., et al. “Drug targeting using thermally responsive polymers and local hyperthermia,” Journal of Controlled Release Jul. 6, 2001; 74: 213-24.

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