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Evidence-Based Complementary and Alternative Medicine
Volume 2017, Article ID 4018724, 10 pages
https://doi.org/10.1155/2017/4018724
Research Article

Interactions of Desmethoxyyangonin, a Secondary Metabolite from Renealmia alpinia, with Human Monoamine Oxidase-A and Oxidase-B

1National Center for Natural Products Research, School of Pharmacy, The University of Mississippi, University, MS 38677, USA
2Department of Biomolecular Sciences, School of Pharmacy, The University of Mississippi, University, MS 38677, USA
3Programa de Ofidismo/Escorpionismo, Sede de Investigación Universitaria, Facultad de Ciencias Farmacéuticas y Alimentarias, Universidad de Antioquia, Torre 2, Laboratorio 631, Medellín, Colombia
4College of Pharmacy, University of South Carolina, Columbia, SC 29208, USA

Correspondence should be addressed to Babu L. Tekwani; ude.ssimelo@inawketb

Received 23 April 2017; Revised 24 June 2017; Accepted 17 July 2017; Published 24 August 2017

Academic Editor: Cheorl-Ho Kim

Copyright © 2017 Narayan D. Chaurasiya et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Renealmia alpinia (Zingiberaceae), a medicinal plant of tropical rainforests, is used to treat snakebites and other injuries and also as a febrifuge, analgesic, antiemetic, antiulcer, and anticonvulsant. The dichloromethane extract of R. alpinia leaves showed potent inhibition of human monoamine oxidases- (MAOs-) A and B. Phytochemical studies yielded six known compounds, including pinostrobin 1, 4′-methyl ether sakuranetin 2, sakuranetin 3, pinostrobin chalcone 4, yashabushidiol A 5, and desmethoxyyangonin 6. Compound 6 displayed about 30-fold higher affinity for MAO-B than MAO-A, with Ki values of 31 and 922 nM, respectively. Kinetic analysis of inhibition and equilibrium-dialysis dissociation assay of the enzyme-inhibitor complex showed reversible binding of desmethoxyyangonin 6 with MAO-A and MAO-B. The binding interactions of compound 6 in the active site of the MAO-A and MAO-B isoenzymes, investigated through molecular modeling algorithms, confirmed preferential binding of desmethoxyyangonin 6 with MAO-B compared to MAO-A. Selective reversible inhibitors of MAO-B, like desmethoxyyangonin 6, may have important therapeutic significance for the treatment of neurodegenerative disorders, such as Parkinson’s disease and Alzheimer’s disease.