Inhibitory kinetics and mechanism of kaempferol on α-glucosidase. (1st January 2016)

• Record Type: Journal Article
• Authors: Peng, Xi; Zhang, Guowen; Liao, Yijing; Gong, Deming
• Is Part Of: Food chemistry. Volume 190(2016)
• Page Start: 207
• Page End: 215
• Publication Date: 2016-01-01
• Subjects: α-Glucosidase -- Kaempferol -- Inhibitory kinetics -- Inhibition mechanism -- Spectroscopy -- Molecular docking; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2015.05.088
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Kaempferol shows effective α-glucosidase inhibition. Kaempferol reversibly inhibits α-glucosidase in a mixed-type manner. Binding of kaempferol with α-glucosidase induces conformational change in latter. Probable inhibition mechanism is elucidated by spectroscopy and molecular docking. 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.