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JOURNALS // Mendeleev Communications // Archive

Mendeleev Commun., 2017 Volume 27, Issue 2, Pages 157–159 (Mi mendc1929)

This article is cited in 2 papers

Communications

Molecular mechanism of interactions between MMP-2 and its oligopeptide-based inhibitors

M. G. Khrenovaab, I. D. Solovyevab, G. D. Lapshina, A. P. Savitskya

a A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russian Federation
b Department of Chemistry, M.V. Lomonosov Moscow State University, Moscow, Russian Federation

Abstract: Taking matrix metalloproteinase MMP-2 as an example, we demonstrate that the rational design of oligopeptide-based inhibitors by molecular modeling should involve both a study of interactions in the active sites of the target enzyme and the conformational dynamics of the oligopeptide in solution.

Language: English

DOI: 10.1016/j.mencom.2017.03.017



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