Abstract

MOLECULAR DOCKING STUDY OF InhA INHIBITORS ON CATECHOL-O-METHYLTRANFERASE

*Shirish Deshpande, Harmish G. Patel

ABSTRACT

Catechol-O-methyltranferase (COMT) is the enzyme that catalyse the transfer of methyl group from S-Adenosyl L- Methionine (SAM) to phenolic group of catecholic molecule. COMT inhibitors are used in the adjunct therapy of Parkinson’s disease. The present investigation is based on the hypothesis that there is active site similarity between the Catechol-O-methyltranferase and enoyl acyl carrier protein reductase (InhA) of Mycobacterium Tuberculosis, enzyme essential for bacterial cell wall synthesis. Docking study performed for two hundred molecules having anti-tubercular activity on COMT enzyme using BioMed CAChe software. Out of them, molecules with best dock score were selected and slight functional group modification were made in some molecules. In silico physicochemical properties like dipole moment, electron affinity, di-electric energy, steric energy, ionization potential, log P, shape index, solvent accessible surface area etc. evaluated by BioMed CAChe software for the selected molecules and Toxicity study like tumorigenicity, mutagenicity, reproductive effect predicted using OSIRIS property explorer.

Keywords: Catechol-O-methyltranferase, Molecular docking, InhA inhibitors, Parkinson’s disease.