title: Comparative docking and CoMFA analysis of curcumine derivatives as HIV-1 integrase inhibitors.
abstract: The docking studies and comparative molecular field analysis (CoMFA) were performed on highly active molecules of curcumine derivatives against 3' processing activity of HIV-1 integrase (IN) enzyme. The optimum CoMFA model was selected with statistically significant cross-validated r(2) value of 0.815 and non-cross validated r (2) value of 0.99. The common pharmacophore of highly active molecules was used for screening of HIV-1 IN inhibitors. The high contribution of polar interactions in pharmacophore mapping is well supported by docking and CoMFA results. The results of docking, CoMFA, and pharmacophore mapping give structural insights as well as important binding features of curcumine derivatives as HIV-1 IN inhibitors which can provide guidance for the rational design of novel HIV-1 IN inhibitors.
authors.affiliation: Centre for Pharmacoinformatics, National Institute of Pharmaceutical Education and Research, Sector-67, S A S Nagar, Punjab 160062, India.
authors.forename: Pawan
authors.initials: P
authors.lastname: Gupta
authors.forename: Prabha
authors.initials: P
authors.lastname: Garg
authors.forename: Nilanjan
authors.initials: N
authors.lastname: Roy
mesh_terms: D001665:Binding Sites; D020134:Catalytic Domain; D003474:Curcumin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000494:pharmacology; D019427:HIV Integrase / Q000737:chemistry / Q000378:metabolism*; D019428:HIV Integrase Inhibitors / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology; D015497:HIV-1 / Q000187:drug effects / Q000201:enzymology; D008958:Models, Molecular; D015394:Molecular Structure; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D021281:Quantitative Structure-Activity Relationship
chemical_list: D019428:HIV Integrase Inhibitors; D019427:HIV Integrase; D003474:Curcumin