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Science 16 August 1991:
Vol. 253. no. 5021, pp. 792 - 795
DOI: 10.1126/science.1876837
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Articles

Science, Vol 253, Issue 5021, 792-795
Copyright © 1991 by American Association for the Advancement of Science

articles

Design and synthesis of a mimetic from an antibody complementarity-determining region

HU Saragovi, D Fitzpatrick, A Raktabutr, H Nakanishi, M Kahn, and MI Greene

Department of Pathology, University of Pennsylvania School of Medicine, Philadelphia 19104.

A technique for producing non-peptide compounds (mimetics) of designed specificities was developed that permitted the synthesis of a conformationally restricted molecule that mimicked the binding and functional properties of monoclonal antibody (MAb) 87.92.6, which recognizes the reovirus type 3 cellular receptor. Binding of either MAb 87.92.6, peptide analogs, or 87.1-mimetic to the cellular receptor inhibited cellular proliferation. The mimetic was a synthetic beta-loop structure that mimics the second complementarity-determining region of the MAb. These studies may lead to strategies for the synthetic design of antibody complementarity regions, ligands, and other pharmacologically active agents that are water soluble, resistant to proteolysis, and nonimmunogenic.


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