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)×10−5molL−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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
