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.
Document Type:
Article
Language: English
Citation:
M. G. Khrenova, I. D. Solovyev, G. D. Lapshin, A. P. Savitsky, “Molecular mechanism of interactions between MMP-2 and its oligopeptide-based inhibitors”, Mendeleev Commun., 27:2 (2017), 157–159
Linking options:
https://www.mathnet.ru/eng/mendc1929
https://www.mathnet.ru/eng/mendc/v27/i2/p157
This publication is cited in the following 2 articles:
A. M. Kulakova, M. G. Khrenova, “Relationship Between Matrix Metalloproteinase-2 Inhibition Constants With APP-IP Oligopeptide and Its Mutant Forms and Electronic Binding Descriptors”, Russ. J. Phys. Chem. B, 15:3 (2021), 394
M. G. Khrenova, V. G. Tsirelson, “The N···H hydrogen bond strength in the transition state at the limiting step determines the reactivity of cephalosporins in the active site of L1 metallo-β-lactamase”, Mendeleev Commun., 29:5 (2019), 492–494
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