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Papers Published

1. Stayton, PS; Chilkoti, A; Long, CJ; Pettit, DK; Tan, PHS; Chen, G; Hoffman, AS, Engineered proteins for biomaterials, Materials Research Society Symposium Proceedings, vol. 292 (January, 1993), pp. 77-82 .
   (last updated on 2024/07/16)

   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.

   Keywords:
   Proteins;Amino acids;Molecules;Antibodies;Polymers;