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  • Title: Inhibitory kinetics and mechanism of kaempferol on α-glucosidase.
    Author: Peng X, Zhang G, Liao Y, Gong D.
    Journal: Food Chem; 2016 Jan 01; 190():207-215. PubMed ID: 26212963.
    Abstract:
    α-Glucosidase is a therapeutic target for diabetes mellitus, and α-glucosidase inhibitors play a vital role in the treatments for the disease. As a kind of potentially safer α-glucosidase inhibitor, flavonoids have attached much attention currently. In this study, kaempferol was found to show a notable inhibition activity on α-glucosidase in a mixed-type manner with IC50 value of (1.16 ± 0.04) × 10(-5) mol L(-1). Analyses of fluorescence, circular dichroism and Fourier transform infrared spectra indicated that kaempferol bound to α-glucosidase with high affinity which was mainly driven by hydrogen bonds and van der Waals forces, and this binding resulted in conformational alteration of α-glucosidase. Further molecular docking study validated the experimental results. It was proposed that kaempferol may interact with some amino acid residues located within the active site of α-glucosidase, occupying the catalytic center of the enzyme to avoid the entrance of p-nitrophenyl-α-D-glucopyranoside and ultimately inhibiting the enzyme activity.
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