Papers Published

  1. Stayton, Patrick S. and Chilkoti, Ashutosh and Long, Cynthia J. and Pettit, Dean K. and Tan, Philip H.S. and Chen, Guohua and Hoffman, Allan S., Engineered proteins for biomaterials, Materials Research Society Symposium Proceedings, vol. 292 (1993), pp. 77 - 82 .
    (last updated on 2007/04/12)

    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.

    Proteins;Amino acids;Molecules;Antibodies;Polymers;