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Tyrosinase inhibitor activity of coumarin-resveratrol hybrids
Antonella Fais1, Marcella Corda, Benedetta Era
1Dipartimento Scienze Applicate ai Biosistemi, Università degli Studi di Cagliari, Cittadella Universitaria di Monserrato, S.S. 554 Km 0.700 bivio per Sestu, 09042 Monserrato, CA, Italy. fais@unica.it
Abstract:
In the present work we report on the contribution of the coumarin moiety to tyrosinase inhibition. Coumarin-resveratrol hybrids 1-8 have been resynthesized to investigate the structure-activity relationships and the IC(50) values of these compounds were measured. The results showed that these compounds exhibited tyrosinase inhibitory activity. Compound 3-(3',4',5'-trihydroxyphenyl)-6,8-dihydroxycoumarin (8)is the most potentcompound (0.27 mM), more so than umbelliferone (0.42 mM), used as reference compound. The kinetic studies revealed that compound 8 caused non-competitive tyrosinase inhibition.
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