کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1372854 | 981885 | 2009 | 4 صفحه PDF | دانلود رایگان |
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.
Molecular docking simulations indicted that parent curcumin binds weakly to xanthine oxidase, while its degradation products exhibit effective inhibitory activities.Figure optionsDownload as PowerPoint slide
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 19, Issue 21, 1 November 2009, Pages 5990–5993