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Development of Biologically Active Peptides Based on Antibody Structure

William V. Williams, David A. Moss, Thomas Kieber-Emmons, Jeffrey A. Cohen, Jeffrey N. Myers, David B. Weiner and Mark I. Greene
Proceedings of the National Academy of Sciences of the United States of America
Vol. 86, No. 14 (Jul. 15, 1989), pp. 5537-5541
Stable URL: http://www.jstor.org/stable/34516
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Development of Biologically Active Peptides Based on Antibody Structure
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Abstract

Antibody molecules are composed of several functional domains, including a variable domain that contacts antigen and a constant domain. The hypervariable regions of antibody molecules play an integral role in determining their specificity. However, the delineation of specific residues most critical in binding is difficult. We have been studying a monoclonal antibody (87.92.6) that binds to the reovirus type 3 receptor on a number of cell types, down-modulates the receptor, and inhibits DNA synthesis in the cells. We have shown that a peptide derived from the second complementarity-determining region of the monoclonal antibody 87.92.6 light-chain variable region can reproduce both of these effects. We were also able to demonstrate specific amino acid residues and structural features involved in producing these effects. The study of antibody structure, coupled with molecular synthetic techniques, can lead to the development of biologically active substances with potential clinical use.

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