IN-SILICO DOCKING STUDIES OF CARBONIC ANHYDRASE INHIBITORS IN THE MANAGEMENT OF NEUROPATHIC PAIN

Abstract

Background: In the present study, the in-silico docking studies of carbonic anhydrase inhibitors with 4RUX i.e. The crystal Structure of Human carbonic Anhydrase II protein was performed in the management of neuropathic pain. Materials and Methods: The crystal structure of protein PDB ID: 4RUX was downloaded from the RCSB PDB database and the ligand molecules of carbonic anhydrase inhibitors were drawn from Marvin Sketch. Docking studies between ligand and protein to predict binding interactions by using AutoDock 4.2 and the receptor-ligand complex interaction viewed by using Biovia Drug Discovery studio. Result: Carbonic anhydrase inhibitors showed binding energy ranging between -5.41 to -8.63. Ganoderic acid A showed better binding energy -8.63 kcal/mol than the standard Acetazolamide -6.22 kcal/mol. Conclusion: The result clearly indicates that among carbonic anhydrase inhibitors, Ganoderic acid A and Morindone show better hydrogen bonding and binding affinity towards carbonic anhydrase II (PDB ID: 4RUX). Thus, conclude that among carbonic anhydrase inhibitors Ganoderic acid A (obtained from Ganoderma lucidium) and Morindone (both obtained from Morinda citrifolia (NONI)} provide the better pharmacological effect.