Docking of Novel Reversible Monoamine Oxidase-B Inhibitors and their Antiparkinsonian Effect

Youssef Moutaouakkil, Ilham Ka

Abstract

Background: Monoamine oxidase is a flavoenzyme responsible for the oxidative deamination of neurotransmitter and dietary amines. Two isozymes of Monoamine oxidase , namely A and B, have been identified on the basis of their substrate preference and inhibitor selectivity. They are the well-known target for antidepressant, Parkinson’s disease and neuroprotective drugs. In this research 3 reversible and Monoamine oxidase B selective inhibitors have been docked computationally to the active site of the MAO-B enzyme in order to demonstrate for the first time the potential of 5-(benzo(b)furan-2- ylmethyl)-6-methylpyridazin-3(2H)-one derives, ability to inhibit MAO-B in comparison with farnesol, one of reversible inhibitors. Methods: 3 reversible and Monoamine oxidase B selective inhibitors were docked with the active site of the Monoamine oxidase B enzyme in order to identify for the first time the potential of 5-(benzo(b)furan-2- ylmethyl)-6-methylpyridazin-3(2H)-one derives, ability to inhibit Monoamine oxidase B. Results and conclusion: The results indicate that 5-(benzo(b)furan-2- ylmethyl)-6-methylpyridazin-3(2H)-one derives could be a good inhibitor for testing in vitro and in vivo against Monoamine oxidase B for treaty Parkinson’s disease.