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 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.
Fais
Antonella
A
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. fais@unica.it
Corda
Marcella
M
Era
Benedetta
B
Fadda
M Benedetta
MB
Matos
Maria Joao
MJ
Quezada
Elias
E
Santana
Lourdes
L
Picciau
Carmen
C
Podda
Gianni
G
Delogu
Giovanna
G
D003374:Coumarins / Q000737:chemistry / Q000494:pharmacology*; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D020128:Inhibitory Concentration 50; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors*; D000077185:Resveratrol; D013267:Stilbenes / Q000737:chemistry / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D003374:Coumarins; D004791:Enzyme Inhibitors; D013267:Stilbenes; C030123:coumarin; D014442:Monophenol Monooxygenase; D000077185:Resveratrol