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Engineered Proteins for Biomaterials

  • Patrick S. Stayton (a1), Ashutosh Chilkoti (a1), Cynthia J. Long (a1), Dean K. Pettit (a1), Philip H. S. Tan (a1), Guohua Chen (a1) and Allan S. Hoffman (a1)...

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.

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Engineered Proteins for Biomaterials

  • Patrick S. Stayton (a1), Ashutosh Chilkoti (a1), Cynthia J. Long (a1), Dean K. Pettit (a1), Philip H. S. Tan (a1), Guohua Chen (a1) and Allan S. Hoffman (a1)...

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