Publication Date:
1991-08-16
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saragovi, H U -- Fitzpatrick, D -- Raktabutr, A -- Nakanishi, H -- Kahn, M -- Greene, M I -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):792-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Pennsylvania School of Medicine, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876837" target="_blank"〉PubMed〈/a〉
Keywords:
Antibodies, Monoclonal/*chemistry
;
Cell Division/drug effects
;
Drug Design
;
Endopeptidases/pharmacology
;
Mammalian orthoreovirus 3
;
Models, Molecular
;
Molecular Conformation
;
Peptides/metabolism
;
Piperidines/chemical synthesis/*chemistry/pharmacology
;
Receptors, Virus/drug effects/*immunology/metabolism
;
Structure-Activity Relationship
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
