MOLECULAR DOCKING AND ADMET STUDIES OF BIOACTIVE COMPOUNDS OF RHIZOPORA MUCORNATA AGAINST BACTERIAL ENZYME PROTEIN TYROSINE PHOSPHATASEAbstract
Objective: The bioactive compounds of Rhizopora mucornata were docked against the bacterial enzyme protein tyrosine phosphatase to determine the potential inhibition. In this research the molecular docking analysis of drug compounds with virulent protein was studied. Material and Methods: Protein Tyrosine phosphatase is an enzyme that is being present in staphylococcus infection that plays an important role in cellular localization, enzyme stability. The target enzyme for Staphylococcus aureus was studied and retrieved from PDB. The bioactive compounds from the leaf extract of Rhizopora mucornata was screened for Lipinski rule of Five and ADMET properties. Autodock 4.2.3 software was used for molecular docking, and the visualization was done by using discovery studio 3.1. Result: The compound 3-methyl-2-(2-oxopropyl) furan shows better binding energy with -1.14 Kcal/mol against the enzyme protein tyrosine phosphatase followed by 3-cyclopentylpropionic acid, 4-methoxyphenyl ester +35.14 Kcal/mol. The hydrogen interactions and Vander Waals interactions, along with total residues of amino acids were studied. This research mainly focuses on targeting the virulent enzyme by using potential drugs to discover a novel therapeutic product.
R. A. Biswal, A. Sharma, A. Aishwariya and V. Pazhamalai *
Department of Bio-Engineering, School of Engineering, Vels Institute of Science, Technology and Advanced Studies (VISTAS), Chennai, Tamil Nadu, India.
26 May 2019
14 October 2019
30 November 2019
01 April 2020