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- W2808362851 abstract "In this work, the hydroxyl-related differences of binding properties and inhibitory activities of dietary flavonoids, namely chrysin, baicalein and apigenin against purine nucleoside phosphorylase (PNP) were investigated. It was found that the hydroxylation on position C4' of chrysin (→apigenin) mildly decreased the binding affinities for PNP, whereas on the position C6 of chrysin (→baicalein) significantly increased binding affinities. Comparatively, the hydroxylation on position C4' and C6 greatly improved their PNP inhibitory effects. The IC50 values of apigenin and baicalein were 6.09 × 10-5 M and 8.94 × 10-5 M, respectively, which is significantly lower than that of chrysin (2.13 × 10-4 M). Results from molecular modeling revealed that there are two binding sites, i.e. active site (major) and tryptophan site (minor) on PNP, and the binding of these flavonoids might induce a serious conformational destabilization of PNP as a result of altering the micro-environment and morphology by flavonoids." @default.
- W2808362851 created "2018-06-21" @default.
- W2808362851 creator A5003781259 @default.
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- W2808362851 date "2018-10-01" @default.
- W2808362851 modified "2023-09-26" @default.
- W2808362851 title "Hydroxyl-related differences for three dietary flavonoids as inhibitors of human purine nucleoside phosphorylase" @default.
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- W2808362851 doi "https://doi.org/10.1016/j.ijbiomac.2018.06.045" @default.
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