Chirattikan MaicheenWeerasak SameeJiraporn UngwitayatornMahidol UniversitySrinakharinwirot University2018-12-212019-03-142018-12-212019-03-142017-10-01Chiang Mai Journal of Science. Vol.44, No.4 (2017), 1395-1406012525262-s2.0-85030712046https://repository.li.mahidol.ac.th/handle/20.500.14594/41756© 2017, Chiang Mai University. All rights reserved. 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 Schäfer et al. Moreover, the potent phthalimides showed the comparable binding affinity to nevirapine toward the enzyme.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyChemistryArticleSCOPUS