Inhibitory kinetics and mechanism of kaempferol on α-glucosidase.

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.

• Authors: Xi Peng, Guowen Zhang, Yijing Liao, Deming Gong
• Journal: Food chemistry (Food Chem) Vol. 190 Pg. 207-215 (Jan 01 2016) ISSN: 1873-7072 [Electronic] England
• PMID: 26212963 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2015 Elsevier Ltd. All rights reserved.

Chemical References

• Flavonoids
• Kaempferols
• kaempferol
• alpha-Glucosidases

Topics

• Flavonoids (chemistry)
• Kaempferols (chemistry)
• Kinetics
• Molecular Docking Simulation (methods)
• Spectrum Analysis (methods)
• alpha-Glucosidases (chemistry, metabolism)