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

Mariya Grigor'evna Khrenova 1, 2
Mariya Grigor'evna Khrenova
, 
Ilya Dmitrievich Solovyev 1, 2
Ilya Dmitrievich Solovyev
, 
Grigory D Lapshin 1
Grigory D Lapshin
, 
Alexander Pavlovich Savitsky 1
Alexander Pavlovich Savitsky
10.1016/j.mencom.2017.03.017
Published 2017-02-27
Communication , Volume 27, Issue 2, 157-159
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Khrenova M. G. et al. Molecular mechanism of interactions between MMP-2 and its oligopeptide-based inhibitors // Mendeleev Communications. 2017. Vol. 27. No. 2. pp. 157-159.
GOST all authors (up to 50) Copy
Khrenova M. G., Solovyev I. D., Lapshin G. D., Savitsky A. P. Molecular mechanism of interactions between MMP-2 and its oligopeptide-based inhibitors // Mendeleev Communications. 2017. Vol. 27. No. 2. pp. 157-159.
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TY - JOUR
DO - 10.1016/j.mencom.2017.03.017
UR - https://mendcomm.colab.ws/publications/10.1016/j.mencom.2017.03.017
TI - Molecular mechanism of interactions between MMP-2 and its oligopeptide-based inhibitors
T2 - Mendeleev Communications
AU - Khrenova, Mariya Grigor'evna
AU - Solovyev, Ilya Dmitrievich
AU - Lapshin, Grigory D
AU - Savitsky, Alexander Pavlovich
PY - 2017
DA - 2017/02/27
PB - Mendeleev Communications
SP - 157-159
IS - 2
VL - 27
ER -
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@article{2017_Khrenova,
author = {Mariya Grigor'evna Khrenova and Ilya Dmitrievich Solovyev and Grigory D Lapshin and Alexander Pavlovich Savitsky},
title = {Molecular mechanism of interactions between MMP-2 and its oligopeptide-based inhibitors},
journal = {Mendeleev Communications},
year = {2017},
volume = {27},
publisher = {Mendeleev Communications},
month = {Feb},
url = {https://mendcomm.colab.ws/publications/10.1016/j.mencom.2017.03.017},
number = {2},
pages = {157--159},
doi = {10.1016/j.mencom.2017.03.017}
}
MLA
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MLA Copy
Khrenova, Mariya Grigor'evna, et al. “Molecular mechanism of interactions between MMP-2 and its oligopeptide-based inhibitors.” Mendeleev Communications, vol. 27, no. 2, Feb. 2017, pp. 157-159. https://mendcomm.colab.ws/publications/10.1016/j.mencom.2017.03.017.

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.

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