Chiang Mai Journal of Science

HIV-1 reverse transcriptase (HIV-1 RT) still remains an important target in the investigation of anti-HIV drugs. A series of synthesized phthalimide derivatives have been previously evaluated for their HIV-1 RT inhibitory activity.  In this study, phthalimide derivatives were subjected to docking study against 6 X-ray crystal structures of wild-type HIV-1 RT using AutoDock software.  Docking results revealed that these phthalimide compounds bound in a similar position and orientation as the clinically used non-nucleoside RT inhibitor (NNRTI), nevirapine.  The bound conformations of the 3 most potent compounds, 11, 25, and 29 with HIV-1 RT were in a roof-like shape, the 3-dimensional pharmacophore for NNRTI proposed by Schfer et al.  Moreover, the potent phthalimides showed the comparable binding affinity to nevirapine toward the enzyme.