Xanthine Oxidase Inhibitory Mechanism of Fisetin and Hesperitin | Journal of Chemical Society of Pakistan 2022

Author(s)

Mengmeng Yu Key Laboratory of Biorheological Science and Technology, Ministry of Education, School of Bioengineering, Chongqing University, Chongqing 400044, China.

Zhongbo Liu School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China.

Liang Jin Key Laboratory of Biorheological Science and Technology, Ministry of Education, School of Bioengineering, Chongqing University, Chongqing 400044, China.

Guizhao Liang Key Laboratory of Biorheological Science and Technology, Ministry of Education, School of Bioengineering, Chongqing University, Chongqing 400044, China.

Abstract

Fisetin and hesperitin are two common flavonoids in plant medicines. In this paper, the mechanism of xanthine oxidase (XO) inhibition was systematically studied by combining experimental and theoretical methods. The HPLC results suggested that the XO inhibitory activity of fisetin (IC50, 0.140 mM) was superior to that of hesperitin (IC50, 0.635 mM). The spectrofluorimetry results showed flavonoids could induce the static fluorescence quenching of XO, indicating that they played the inhibitory activity by forming the complexes with XO. We showed the paramount force of fisetin and XO was hydrophobic; in the complex of hesperidin and XO, hydrogen bonding and van der Waals force were crucial forces. We used Autodock software for molecular docking. The results suggested that both fisetin and hesperitin entered the active pocket of XO, and the complexes were maintained by hydrogen bonding and hydrophobic interaction, which coincided with the experimental results.

Publication Details

Page(s) 78-83

DOI DOI not available

Published Journal: Journal of Chemical Society of Pakistan, Volume: 44, Issue: 1, Year: 2022

Keywords

molecular docking Spectrofluorimetry Xanthine oxidase interaction Fisetin Hesperitin

References

References are not available for this document.

Citations

Citations are not available for this document.