α-Glucosidase Inhibitors from Vauquelinia corymbosa

Molecules

Laura Flores-Bocanegra²  Araceli Pérez-Vásquez²  Mariana Torres-Piedra²  Robert Bye¹  Edelmira Linares¹  Rachel Mata² 

[1] Instituto de Biología, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico; E-Mails:;Facultad de Química, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico; E-Mails:

关键词: diabetes;    yeast and rat α-glucosidases;    Vauquelinia corymbosa;   

DOI  :  10.3390/molecules200815330

来源: mdpi

【 摘 要 】

The 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 (K_i) 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.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.