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- W2012109757 abstract "Abstract HIV-1 protease has been an attractive drug target for the antiretroviral treatment of HIV infection over the years. Molecular dynamics (MD) simulations coupled with Molecular Mechanics Poisson–Boltzmann Surface Area (MM-PB/SA) method have been carried out to investigate the bindings of inhibitors BEC and BEG to HIV-1 protease. The results suggest that van der Waals energies mostly drive the binding of this class of inhibitors to HIV-1 protease. The analyses of structure–affinity relationship by using the free energy decomposition provide a more-detailed insight into the mechanisms driving the bindings of BEC and BEG to HIV-1 protease. It is found that a number of C–H…π and C–H…H–C interactions exist between the hydrophobic groups of BEC and BEG and the hydrophobic residues of the binding pocket in HIV-1 protease, and these interactions and the hydrogen bond interactions of BEC and BEG with HIV-1 protease play important roles in the bindings of BEC and BEG to HIV-1 protease. The improvement and optimization of these interactions are helpful to the rational design of potent inhibitors combating AIDS." @default.
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- W2012109757 date "2009-11-01" @default.
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- W2012109757 title "Molecular insight into the interaction mechanisms of inhibitors BEC and BEG with HIV-1 protease by using MM-PBSA method and molecular dynamics simulation" @default.
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- W2012109757 doi "https://doi.org/10.1016/j.theochem.2009.07.010" @default.
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