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

Article in Evidence-based Complementary and Alternative Medicine 2017(2):1-10 · August 2017 DOI: 10.1155/2017/4018724 · License: CC BY 4.0 1st Narayan D Chaurasiya 29.91 · University of Mississippi 2nd Francisco León 36.12 · University of Florida + 4 3rd Yuanqing Ding Last Babu Tekwani 44.32 · University of Mississippi Show more authors 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 Interactions of Desmethoxyyangonin, a Secondary Metabolite from Renealmia alpinia , with Human Monoamine Oxidase-A and Oxidase-B. Available from: https://www.researchgate.net/publication/319279512_Interactions_of_Desmethoxyyangonin_a_Secondary_Metabolite_from_Renealmia_alpinia_with_Human_Monoamine_Oxidase-A_and_Oxidase-B [accessed Aug 29, 2017].