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- W2116718902 abstract "The aim was to assess the inhibitory effect of a series of naturally occurring trans-resveratrol analogues on cytochromes P450, namely CYP1A2 and CYP2E1, in vitro in order to analyse any structure–activity relationships. 3,5-Dimethoxy-4′-hydroxy-trans-stilbene (pterostilbene), 3,4′,5-trimethoxy-trans-stilbene (TMS), 3,4′-dihydroxy-5-methoxy-trans-stilbene (3,4′-DH-5-MS) and 3,5-dihydroxy-4′-methoxy-trans-stilbene (3,5-DH-4′-MS) inhibited the activity of CYP1A2, with Ki = 0.39, 0.79, 0.94 and 1.04 µM, respectively. Piceatannol (3,3′,4,5′-tetrahydroxy-trans-stilbene) was the least potent inhibitor of CYP1A2 with a Ki = 9.67 µM. Piceatannol and TMS in the concentration range 1–100 µM did not inhibit CYP2E1 activity. The activity of this enzyme likewise was not significantly influenced by pterostilbene and 3,5-DH-4′-MS with IC50 > 100 µM, whereas 3,4′-DH-5-MS appeared to be a moderately potent, competitive inhibitor of CYP2E1 (Ki = 42.6 µM). Structure–activity relationship analysis leads to the conclusion that the substitution of hydroxy groups of resveratrol with methoxy groups increases the inhibition of CYP1A2, yet the number and position of methylation are not essential. However, the 4′-hydroxy group in trans-resveratrol and its analogues may play an important role in the interaction with a binding site of CYP2E1." @default.
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- W2116718902 date "2006-04-01" @default.
- W2116718902 modified "2023-10-18" @default.
- W2116718902 title "Effect of natural analogues of<b><i>trans</i></b>-resveratrol on cytochromes P4501A2 and 2E1 catalytic activities" @default.
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- W2116718902 doi "https://doi.org/10.1080/00498250500485057" @default.
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