MOLECULAR DOCKING AND ADMET STUDIES OF ETHANONE, 1-(2-HYDROXY-5-METHYL PHENYL) FOR ANTI-MICROBIAL PROPERTIES

Abstract

Objective: Ethanone 1-(2-hydroxy-5-methyl phenyl) found in the aerial parts of Rhizophora mucronate, Epiphyllum oxypetalum haw and dried ripened seed extracts of coffee. It has reported anti-microbial properties based on the literature. The objective of the present study is to find the binding efficacy of the compound with proteins in staphylococcus aureus and to report the ADMET properties of the compound.

Methods: Rigid docking technique was used for finding the affinities.3D structures of the six proteins of staphylococcus aureus are selected from the protein database. Molecule Ethanone 1-(2-hydroxy-5-methyl phenyl) is obtained from PubChem. ADMET studies of the compound are assessed by SWISS-ADME. Molecular docking studies are carried out by using PyRx software.

Results: Ethanone 1-(2-hydroxy-5-methyl phenyl) on molecular docking with Staphylococcus aureus sortase-A (PDB ID: 1T2P), Clumping factor A (ClfA) (PDB ID: 1N67), DNA gyrase (PDB ID: 3U2D), Dihydrofolate reductase (DHFR) (PDB ID: 2W9S), Undecaprenyl diphosphate synthase (UPPS) (PDB ID: 4H8E), Dehydrosqualene synthase (CrtM) (PDB ID: 2ZCO), their binding affinities were found to be-6.2,-6.3,-5.9,-6.4,-5.3,-6.8 respectively. Out of six proteins, Dehydrosqualene synthase (CrtM) (PDB ID: 2ZCO) and Dihydrofolate reductase (DHFR) (PDB ID: 2W9S) has shown better binding affinities.

Conclusion: ADMET studies show that Ethanone 1-(2-hydroxy-5-methyl phenyl) has zero violation to Lipinski’s rule and molecular docking with two proteins has shown good binding efficacy with Ethanone 1-(2-hydroxy-5-methylphenyl).