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A Comparative Insight into Amprenavir Resistance of Mutations V32I, G48V, I50V, I54V, and I84V in HIV-1 Protease Based on Thermodynamic Integration and MM-PBSA Methods.

Journal of chemical information and modeling - 28 Sept 2015

Chen Jianzhong, Wang Xingyu, Zhu Tong, Zhang Qinggang, Zhang John Z H

Abstract excerpt

Drug resistance of mutations V32I, G48V, I50V, I54V, and I84V in HIV-1 protease (PR) was found in clinical treatment of HIV patients with the drug amprenavir (APV). In order to elucidate the molecular mechanism of drug resistance associated with these mutations, the thermodynamic integration (TI) and molecular mechanics Poisson-Boltzmann surface area (MM-PBSA) methods were applied to calculate binding free...

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Anti-HIV Agents
Carbamates
Drug Resistance, Viral
Furans
Hydrogen Bonding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Dynamics Simulation

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PMID: 26317593
DOI: 10.1021/acs.jcim.5b00173

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