2. Academic Validation
  3. Interactions of Desmethoxyyangonin, a Secondary Metabolite from Renealmia alpinia, with Human Monoamine Oxidase-A and Oxidase-B

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

  • Evid Based Complement Alternat Med. 2017:2017:4018724. doi: 10.1155/2017/4018724.
Narayan D Chaurasiya 1,  Francisco León 2,  Yuanqing Ding 1,  Isabel Gómez-Betancur 3,  Dora Benjumea 3,  Larry A Walker 1 2,  Stephen J Cutler 1 4,  Babu L Tekwani 1 2
Affiliations

Affiliations

  • 1 National Center for Natural Products Research, School of Pharmacy, The University of Mississippi, University, MS 38677, USA.
  • 2 Department of Biomolecular Sciences, School of Pharmacy, The University of Mississippi, University, MS 38677, USA.
  • 3 Programa de Ofidismo/Escorpionismo, Sede de Investigación Universitaria, Facultad de Ciencias Farmacéuticas y Alimentarias, Universidad de Antioquia, Torre 2, Laboratorio 631, Medellín, Colombia.
  • 4 College of Pharmacy, University of South Carolina, Columbia, SC 29208, USA.
PMID: 29138643 DOI: 10.1155/2017/4018724
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.

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