Patcharawee NunthanavanitJiraporn UngwitayatornSrinakharinwirot UniversityMahidol University2018-11-092018-11-092014-08-05Medicinal Chemistry Research. Vol.23, No.9 (2014), 4198-420815548120105425232-s2.0-84896434812https://repository.li.mahidol.ac.th/handle/20.500.14594/33618© 2014 Springer Science+Business Media New York. Developing a new HIV-1 protease (HIV-1 PR) inhibitor is still a challenging task to overcome the drug resistance mutations in the HIV-PR. In this study, docking simulations of chromone derivatives against wild type and eleven mutant variants HIV-1 PR were investigated using GOLD and Autodock programs. From both GOLD and Autodock results, chromone 3, the experimentally observed highly potent HIV-1 PR inhibitor, showed stronger binding affinity against every studied mutant strain (2AVS, 2AVO, 2AVV, 1MES, 1MET, 1MEU, 1SDU, 1SDV, 1C6Y, 2F8O, and 1SH9) than the wild-type enzyme (1AJX). Chromone 32, another potent inhibitor as well as chromones 33, 34, 37, and 47 also showed high binding interaction with several mutant-type enzymes. The coherent picture of the interactions at the active sites of mutant PR should facilitate the further design and development of new potent inhibitor against multidrug-resistant virus.Mahidol UniversityChemistryPharmacology, Toxicology and PharmaceuticsArticleSCOPUS10.1007/s00044-014-0992-2