Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 63, Issue 2, Pages 526-534Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf505584m
Keywords
xanthine oxidase; kaempferol; inhibition mechanism; spectroscopy; molecular simulation
Funding
- National Natural Science Foundation of China [21167013, 31460422, 31060210]
- Natural Science Foundation of Jiangxi Province [20142BAB204001, 20143ACB20006]
- Joint Specialized Research Fund for the Doctoral Program of Higher Education [20123601110005]
- Program of Jiangxi Provincial Department of Science and Technology [20141BBG70092]
- Research Program of State Key Laboratory of Food Science and Technology of Nanchang University [SKLF-ZZB-201305, SKLF-ZZA-201302, SKLF-KF-201203]
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Xanthine oxidase (XO), a key enzyme in purine catabolism, is widely distributed in human tissues. It can catalyze xanthine to generate uric acid and cause hyperuricemia and gout. Inhibition kinetics assay showed that kaempferol inhibited XO activity reversibly in a competitive manner. Strong fluorescence quenching and conformational changes of XO were found due to the formation of a kaempferol-XO complex, which was driven mainly by hydrophobic forces. The molecular docking further revealed that kaempferol inserted into the hydrophobic cavity of XO to interact with some amino acid residues. The main inhibition mechanism of kaempferol on XO activity may be due to the insertion of kaempferol into the active site of XO occupying the catalytic center of the enzyme to avoid the entrance of the substrate and inducing conformational changes of XO. In addition, luteolin exhibited a stronger synergistic effect with kaempferol than did morin at the lower concentration.
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