期刊
FOOD CHEMISTRY
卷 141, 期 4, 页码 3766-3773出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2013.06.092
关键词
Luteolin; Xanthine oxidase; Inhibition kinetics; Fluorescence quenching; Circular dichroism; Molecular simulation
资金
- National Natural Science Foundation of China [31060210, 21167013]
- Natural Science Foundation of Jiangxi Province [20114BAB204019]
- Research Program of State Key Laboratory of Food Science and Technology of Nanchang University [SKLF-ZZB-201305, SKLF-ZZA-201302, SKLF-KF-201203]
- Program of Jiangxi Provincial Department of Science and Technology [2009BNA09000, 2010BSA17400, 20112BBF60010]
Xanthine oxidase (XO) catalyses hypoxanthine and xanthine to uric acid in human metabolism. Overproduction of uric acid will lead to hyperuricemia and finally cause gout and other diseases. Luteolin is one of the major components of celery and green peppers, its inhibitory activity on XO and their interaction mechanism were evaluated by multispectroscopic methods, coupled with molecular simulation. It was found that luteolin reversibly inhibited XO in a competitive manner with inhibition constant (K-i) value of (2.38 +/- 0.05) x 10(-6) mol l(-1). Luteolin could bind to XO at a single binding site and the binding was driven mainly by hydrophobic interactions. Analysis of synchronous fluorescence and circular dichroism spectra demonstrated that the microenvironment and secondary structure of XO were altered upon interaction with luteolin. The molecular docking results revealed luteolin actually interacted with the primary amino acid residues located within the active site pocket of XO. (C) 2013 Elsevier Ltd. All rights reserved.
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