Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5417294 | Journal of Molecular Structure: THEOCHEM | 2009 | 6 Pages |
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-Hâ¦Ï and C-Hâ¦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.
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Shu-Hua Shi, Jian-Zhong Chen, Guo-Dong Hu, Chang-Hong Yi, Shao-Long Zhang, Qing-Gang Zhang,