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Idescarpin Isolated from the Fruits of Idesia polycarpa Inhibits Melanin Biosynthesis

Seung‐Hwa Baek, Dong‐Hyun Kim, Chanyong Lee, Yung‐Hee Kho, Choonghwan Lee

Open publisher page 19 citations

Abstract

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.

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What this paper is about

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.

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Available abstract

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.

Key concepts: Tyrosinase, Melanin, Biosynthesis, Skin whitening, Biochemistry, Inhibitory postsynaptic potential, Chemistry, Enzyme

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