Insights into the inhibition of xanthine oxidase by curcumin.
As a natural pigment, curcumin exhibits multiple biological activities. Previous studies have investigated the inhibition of xanthine oxidase (XO) by curcumin. In the present work, based on the molecular docking simulations, it is interesting to find that parent curcumin binds weakly to XO, while its degradation products, for example, trans-6-(4'-hydroxy-3'-methoxyphenyl)-2,4-dioxo-5-hexenal, exhibit effective inhibitory activities against XO. The findings shed new light on the underlying mechanisms of curcumin in inhibiting XO and also have potential implication that both parent curcumin and its degradation products should be taken into account when exploring the mechanisms of curcumin's biological activities.
Shen
Liang
L
Shandong Provincial Research Center for Bioinformatic Engineering and Technique, Center for Advanced Study, Shandong University of Technology, Zibo 255049, PR China.
Ji
Hong-Fang
HF
D000975:Antioxidants / Q000737:chemistry* / Q000494:pharmacology; D001665:Binding Sites; D003198:Computer Simulation; D003474:Curcumin / Q000737:chemistry* / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology; D014969:Xanthine Oxidase / Q000037:antagonists & inhibitors* / Q000378:metabolism
D000975:Antioxidants; D004791:Enzyme Inhibitors; D014969:Xanthine Oxidase; D003474:Curcumin