| Cellular activities and docking studies of eckol isolated from Ecklonia cava (Laminariales, Phaeophyceae) as potential tyrosinase inhibitor
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| Seung-Hong Lee1, Sung-Myung Kang2, Chang Hyun Sok3, Jin Tae Hong3, Jae-Young Oh4 and You-Jin Jeon4,*
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1Division of Food Bioscience and Korea Nokyong Research Center, Konkuk University, Chungju 380-701, Korea
2Department of Anatomy and Cell Biology, University of Calgary, Faculty of Medicine, Calgary, Alberta T2N 1N4, Canada
3College of Pharmacy, Chungbuk National University, Cheongju 362-763, Korea
4Department of Marine Life Science, Jeju National University, Jeju 690-756, Korea
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| ABSTRACT |
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Tyrosinase inhibitors are an important component of cosmetic products. Our previous studies have proposed that eckol isolated from the brown alga Ecklonia cava, can be explored as a tyrosinase inhibitor. However, cellular activities and mechanism of action of eckol remain unknown. Therefore, the current study analyzed the eckol binding modes using the crystal structure of Bacillus megaterium tyrosinase. The effects of eckol on melanin synthesis induced by α-melanocyte stimulating hormone in B16F10 melanoma cells were also investigated. We predicted the 3D structure of tyrosinase and used a docking algorithm to simulate binding between tyrosinase and eckol. These molecular modeling studies were successful (calculated binding energy value, -115.84 kcal mol-1) and indicated that eckol interacts with Asn205, His208, and Arg209. Furthermore, eckol markedly inhibited tyrosinase activity and melanin synthesis in B16F10 melanoma cells. We also found that eckol decreased the expression of tyrosinase, tyrosinase-related protein (TRP) 1, and TRP2. These results indicate that eckol is a potent inhibitor of melanogenesis, and this finding may be useful for the development of novel pharmaceutical and cosmetic agents.
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| Key words:
B16F10 melanoma cells; eckol; melanin synthesis; molecular docking; tyrosinase |
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