α-Glucosidase Inhibitors from Vauquelinia corymbosa
AbstractThe α-glucosidase inhibitory activity of an aqueous extract and compounds from the aerial parts of V. corymbosa was demonstrated with yeast and rat small intestinal α-glucosidases. The aqueous extract inhibited yeast α-glucosidase with a half maximal inhibitory concentration (IC50) of 28.6 μg/mL. Bioassay-guided fractionation of the extract led to the isolation of several compounds, including one cyanogenic glycoside [prunasin (1)], five flavonoids [(−)-epi-catechin (2), hyperoside (3), isoquercetin (4), quercitrin (5) and quercetin-3-O-(6′′-benzoyl)-β-galactoside (6)] and two simple aromatic compounds [picein (7) and methylarbutin (8)]. The most active compound was 6 with IC50 values of 30 μM in the case of yeast α-glucosidase, and 437 μM in the case of the mammalian enzyme. According to the kinetic analyses performed with rat and yeast enzymes, this compound behaved as mixed-type inhibitor; the calculated inhibition constants (Ki) were 212 and 50 μM, respectively. Molecular docking analyses with yeast and mammalian α-glucosidases revealed that compound 6 bind differently to these enzymes. Altogether, the results of this work suggest that preparations of V. corymbosa might delay glucose absorption in vivo. View Full-Text
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Flores-Bocanegra, L.; Pérez-Vásquez, A.; Torres-Piedra, M.; Bye, R.; Linares, E.; Mata, R. α-Glucosidase Inhibitors from Vauquelinia corymbosa. Molecules 2015, 20, 15330-15342.
Flores-Bocanegra L, Pérez-Vásquez A, Torres-Piedra M, Bye R, Linares E, Mata R. α-Glucosidase Inhibitors from Vauquelinia corymbosa. Molecules. 2015; 20(8):15330-15342.Chicago/Turabian Style
Flores-Bocanegra, Laura; Pérez-Vásquez, Araceli; Torres-Piedra, Mariana; Bye, Robert; Linares, Edelmira; Mata, Rachel. 2015. "α-Glucosidase Inhibitors from Vauquelinia corymbosa." Molecules 20, no. 8: 15330-15342.