Intermolecular force between monoamine oxidase B and Pseudarthria viscida (L.) using atomic force spectroscopy

Abstract

Inhibition of monoamine oxidase B (MAO-B) activity by deprenyl hydrochloride (drug) and methanolic extract of Pseudarthria viscida (L.) have been studied using atomic force microscopy force-distance (AFM F-D) curves. Attractive force measured between MAO-B and kynuramine dihydrobromide (substrate) was 56.12 pN ± 8.9, between MAO-B (inhibited by drug) and substrate was 11.25 pN ± 2.6 and MAO-B (inhibited by plant extract) and substrate was 18.61 pN ± 2.9. Phytochemical analysis revealed catechin as one of the compounds in P. viscida (L.) extract and MAO-B-catechin binding sites were confirmed using in silico methods. This study is perhaps the first report of combining three techniques, namely AFM F-D curves, phytochemical and in silico analysis to measure enzyme-substrate attractive force, constituents of plant extract and position of binding sites, respectively. © 2013 Copyright Taylor and Francis Group, LLC.