The Effect of Geometrical Isomerism of 3,5-Dicaffeoylquinic Acid on Its Binding Affinity to HIV-Integrase Enzyme: A Molecular Docking Study.

ABSTRACT: A potent plant-derived HIV-1 inhibitor, 3,5-dicaffeoylquinic acid (diCQA), has been shown to undergo isomerisation upon UV exposure where the naturally occurring 3 ^trans ,5 ^trans -diCQA isomer gives rise to the 3 ^cis ,5 ^trans -diCQA, 3 ^trans ,5 ^cis -diCQA, and 3 ^cis ,5 ^cis -diCQA isomers. In this study, inhibition of HIV-1 INT by UV-induced isomers was investigated using molecular docking methods. Here, density functional theory (DFT) models were used for geometry optimization of the 3,5-diCQA isomers. The YASARA and Autodock VINA software packages were then used to determine the binding interactions between the HIV-1 INT catalytic domain and the 3

SUBMITTER: Makola MM 

PROVIDER: S-EPMC5088326 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature