Open AccessMultiple Molecular Dynamics Simulations and Energy Analysis Unravel the Dynamic Properties and Binding Mechanism of Mutants HIV-1 Protease with DRV and CA-p2
Author(s) -
Ruige Wang,
QingChuan Zheng
Publication year - 2022
Publication title -
microbiology spectrum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.502
H-Index - 51
ISSN - 2165-0497
DOI - 10.1128/spectrum.00748-21
Subject(s) - darunavir , molecular dynamics , protease , mutant , chemistry , biophysics , binding site , hiv 1 protease , substrate (aquarium) , ligand (biochemistry) , human immunodeficiency virus (hiv) , stereochemistry , binding energy , combinatorial chemistry , biochemistry , computational chemistry , biology , virology , enzyme , antiretroviral therapy , physics , gene , ecology , receptor , viral load , nuclear physics
Developing effective anti-HIV inhibitors is the current requirement to cope with the emergence of the resistance of mutants. Compared with the experiments, MD simulations along with energy calculations help reduce the time and cost of designing new inhibitors. Based on our simulation results, we propose two factors that may help design effective inhibitors against HIV-1 PR: (i) importance of hydrophobic cavity, and (ii) introduction of polar groups similar to the guanidine group.