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Molecules 2009, 14(7), 2514-2520;

Tyrosinase Inhibitor Activity of Coumarin-Resveratrol Hybrids

Dipartimento 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
Departamento de Química Orgánica, Facultade de Farmacia, Universidade de Santiago de Compostela, 15782 Santiago de Compostela, Spain
Dipartimento Farmaco Chimico Tecnologico, Università degli Studi di Cagliari, Via Ospedale 72, 09124 Cagliari, CA, Italy
Authors to whom correspondence should be addressed.
Received: 11 May 2009 / Revised: 9 July 2009 / Accepted: 10 July 2009 / Published: 13 July 2009
(This article belongs to the Special Issue Coumarins and Xanthones)
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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 IC50 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. View Full-Text
Keywords: tyrosinase inhibitors; resveratrol; coumarins tyrosinase inhibitors; resveratrol; coumarins

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This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Fais, A.; Corda, M.; Era, B.; Fadda, M.B.; Matos, M.J.; Quezada q, E.; Santana, L.; Picciau, C.; Podda, G.; Delogu, G. Tyrosinase Inhibitor Activity of Coumarin-Resveratrol Hybrids. Molecules 2009, 14, 2514-2520.

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