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Engineered Proteins for Biomaterials

Published online by Cambridge University Press:  15 February 2011

Patrick S. Stayton ,
Ashutosh Chilkoti ,
Cynthia J. Long ,
Dean K. Pettit ,
Philip H. S. Tan ,
Guohua Chen  and
Allan S. Hoffman
Patrick S. Stayton
Affiliation:
Center for Bioengineering, WD- 12, University of Washington, Seattle, WA 98195
Ashutosh Chilkoti
Affiliation:
Center for Bioengineering, WD- 12, University of Washington, Seattle, WA 98195
Cynthia J. Long
Affiliation:
Center for Bioengineering, WD- 12, University of Washington, Seattle, WA 98195
Dean K. Pettit
Affiliation:
Center for Bioengineering, WD- 12, University of Washington, Seattle, WA 98195
Philip H. S. Tan
Affiliation:
Center for Bioengineering, WD- 12, University of Washington, Seattle, WA 98195
Guohua Chen
Affiliation:
Center for Bioengineering, WD- 12, University of Washington, Seattle, WA 98195
Allan S. Hoffman
Affiliation:
Center for Bioengineering, WD- 12, University of Washington, Seattle, WA 98195
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Abstract

A molecular adaptor for interfacing environmentally sensitive, soluble polymers and antibody molecules has been developed. The gene coding for the minimally sized, 55 amino acid IgG binding domain from protein G has been constructed by total gene synthesis. This domain is thermally stable, exhibits a highly reversible folding and unfolding equilibrium, and recognizes IgG and Fab molecules with high affinity. These properties make the protein G domain a potentially useful adaptor for non-covalent immobilization of antibodies to soluble polymers and hydrogels. Engineered single-chain Fv antibody fragments have also been constructed and a method for expanding the usefulness of the protein G adaptor to these molecules is proposed. The engineered antibodies also provide a model system for developing general immobilization strategies aimed at maximizing binding affinities and therapeutic responses. The overall goal is to develop optimized engineering designs for functionally optimized antibody-material hybrids.

Information

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 292: Symposium S – Biomolecular Materials , 1992 , 77
Copyright
Copyright © Materials Research Society 1993

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