Tyrosinase Inhibitor Activity of Coumarin-Resveratrol Hybrids

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 compou...

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Detalles Bibliográficos
Autores principales: Fais, Antonella, Corda, Marcella, Era, Benedetta, Fadda, M. Benedetta, Matos, Maria Joao, Quezada, Elias, Santana, Lourdes, Picciau, Carmen, Podda, Gianni, Delogu, Giovanna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International 2009
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Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6255045/
https://www.ncbi.nlm.nih.gov/pubmed/19633620
http://dx.doi.org/10.3390/molecules14072514
Descripción
Sumario: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 potent compound (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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