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Theoretical studies of energetics and binding isotope effects of binding a triazole-based inhibitor to HIV-1 reverse transcriptase

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Abstract

Understanding of protein-ligand interactions is crucial for rational drug design. Binding isotope effects, BIEs, can provide intimate details of specific interactions between individual atoms of an inhibitor and the binding pocket. We have applied multi-scale QM/MM simulations to evaluate binding energetics of a novel triazole-based non-nucleoside inhibitor of HIV-1 reverse transcriptase and to calculate associated BIEs. The binding sites can be distinguished based on the 18O-BIE.

Graphical abstract: Theoretical studies of energetics and binding isotope effects of binding a triazole-based inhibitor to HIV-1 reverse transcriptase

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Article information


Submitted
08 Oct 2015
Accepted
20 Nov 2015
First published
20 Nov 2015

This article is Open Access

Phys. Chem. Chem. Phys., 2016,18, 310-317
Article type
Paper
Author version available

Theoretical studies of energetics and binding isotope effects of binding a triazole-based inhibitor to HIV-1 reverse transcriptase

A. Krzemińska, K. P. Świderek and P. Paneth, Phys. Chem. Chem. Phys., 2016, 18, 310
DOI: 10.1039/C5CP06050H

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