1. Xanthones from Gentianella amarella ssp. acuta with acetylcholinesterase and monoamine oxidase inhibitory activities.
- Author
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Urbain A, Marston A, Grilo LS, Bravo J, Purev O, Purevsuren B, Batsuren D, Reist M, Carrupt PA, and Hostettmann K
- Subjects
- Cholinesterase Inhibitors chemistry, Glucosides, Glycosides chemistry, Molecular Structure, Mongolia, Monoamine Oxidase Inhibitors chemistry, Nuclear Magnetic Resonance, Biomolecular, Xanthones chemistry, Cholinesterase Inhibitors isolation & purification, Cholinesterase Inhibitors pharmacology, Gentianella chemistry, Glycosides isolation & purification, Glycosides pharmacology, Monoamine Oxidase Inhibitors isolation & purification, Monoamine Oxidase Inhibitors pharmacology, Plants, Medicinal chemistry, Xanthones isolation & purification, Xanthones pharmacology
- Abstract
Two new xanthone glycosides, corymbiferin 3-O-beta-D-glucopyranoside (1) and swertiabisxanthone-I 8'-O-beta- d-glucopyranoside (2), were isolated from Gentianella amarella ssp. acuta, along with eight known xanthones: triptexanthoside C, veratriloside, corymbiferin 1-O-glucoside, swertianolin, norswertianolin, swertiabisxanthone-I, bellidin, and bellidifolin, four of them identified for the first time in G. amarella ssp. acuta. The isolation was conducted mainly by centrifugal partition chromatography, and the structures of the isolated compounds were established on the basis of spectrometric data including 2D NMR and mass spectrometry. Xanthones were weakly active against acetylcholinesterase (AChE), except triptexanthoside C, which inhibited AChE with an IC(50) of 13.8 +/- 1.6 microM. Some compounds were active against monoamine oxidases (MAO): bellidin and bellidifolin showed interesting inhibitory activity of MAO A, while swertianolin, the 8-O-glucopyranoside form of bellidifolin, gave 93.6% inhibition of MAO B activity at 10(-5) M.
- Published
- 2008
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