Vibrational Analysis and Molecular Docking Studies on some Ribonuclease-H HIV Inhibitors

Abstract

Ribonuclease-H (RNase-H) enzyme of the human immunodeficiency virus (HIV) reverse transcriptase (RT) shows inhibitory activity with novel galloyl derivatives having enzymatic assays of IC50 S at sub to low micromolar concentration. The computational analysis of these stated galloyl derivatives was carried out in order to extract information and performance with the target proteins. The compounds N-hydroxylisoquinolinediones (HID), β-thujaplicinol, diketoacid, diketoacid ester, pyrimidinol carboxylic acids, naphthyridinones, 3hydroxypyrimidine-2,4-dione (HPD), and hydroxypyridonecarboxylic acids are the selected galloyl derivatives of human immunodeficiency virus-I (HIV-I) RNase-H active site inhibitors that were optimized using Turbomole software. Further evaluation of their NMR shielding of the stated compounds was performed using B3-LYP hybrid functional, and the def-SV basis set was carried out from the same software. These optimized compounds were then docked to targets (PDB Id: 5EGA and 3K2P) using AutoDock 4 software. After analyzing the docking result, Hydroxylisoquinoline and Naphthyridinones give better binding results with both the targets.