Idescarpin isolated from the fruits of Idesia polycarpa inhibits melanin biosynthesis

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Idescarpin isolated from the fruits of Idesia polycarpa inhibits melanin biosynthesis
Seunghwa Baek; D Kim; C Lee; Yung Hee Kho; Choong Hwan Lee
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 16, no. 5, pp. 667-672
Publication Year
Tyrosinase is an enzyme that catalyzes the biosynthetic pathway of melanin pigments participating in the coloring of skin, hair, and eyes, and is widely distributed in nature. The inhibitory compounds of tyrosinase have been extensively used as a cosmetic agent with a skin-whitening effect. In this paper, several plant extracts were screened using Melan-a cells for the melanin biosynthesis inhibition activity, and Idesia polycarpa was selected. A melanin biosynthesis inhibitor was isolated from I. polycarpa fruits by activity-guided fractionation, and the inhibitor was identified as 6-hydroxy-2- [(1-hydr oxy-6-oxo-2-cyclohexen-1-yl)carbonyl]oxy]methyl]phenyl β-D-glucopyranoside (idescrapin) by comparing it with reported spectral data. Idescarpin (IC50 = 8 μg/ml) reduced melanin content compared with the vehicle. In addition, the inhibitory activity of idescarpin for melanin synthesis is mediated by decreasing tyrosinase protein rather than directly inhibiting the tyrosinase activity. These results suggest that idescarpin isolated from I. polycarpa fruits may be used as a skin-whitening agent.
idescarpinidesia polycarpamelana cellmelanin biosynthesis inhibitorskin-whiteningtyrosinase
Korea Soc-Assoc-Inst
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