Natural Product Sciences

The Korean Society of Pharmacognosy (한국생약학회)
권호 표지

Tyrosinase Inhibitory Constituents of Morus bombycis Cortex

  • Kang, Kyo-Bin (College of Pharmacy and Research Institute of Pharmaceutical Science, Seoul National University) ;
  • Kim, Sang-Du (College of Pharmacy and Research Institute of Pharmaceutical Science, Seoul National University) ;
  • Kim, Tae-Bum (College of Pharmacy and Research Institute of Pharmaceutical Science, Seoul National University) ;
  • Jeong, Eun-Ju (College of Pharmacy and Research Institute of Pharmaceutical Science, Seoul National University) ;
  • Kim, Young-Choong (College of Pharmacy and Research Institute of Pharmaceutical Science, Seoul National University) ;
  • Sung, Jong-Hyuk (CHA stem cell institutes, CHA University) ;
  • Sung, Sang-Hyun (College of Pharmacy and Research Institute of Pharmaceutical Science, Seoul National University)
  • Received : 2011.05.12
  • Accepted : 2011.08.15
  • Published : 2011.09.30
Download PDF
⟨ Previous Next ⟩

Abstract

Tyrosinase is one of the important enzymes in the mammalian melanin synthesis. In the process of melanin synthesis, tyrosine is oxidized to DOPA (3,4-dihydroxyphenylalanine), and DOPA is further oxidized to dopaquinone. Tyrosinase is an enzyme catalyzing this oxidation of tyrosine, so chemicals that inhibit the activity of tyrosinase can be used as skin whitening agents. In this study, we isolated five constituents from the 80% MeOH extract of Morus bombycis cortex by bioactivity-guided fractionation. We performed mushroom tyrosinase inhibition assay. As a result, 7,2',4'-trihydroxyflavanone (1), 2',4',2,4,-tetrahydroxychalcone (2), and oxyresveratrol (3) showed the more potent inhibitory effect compared to kojic acid, a well-known skin whitening agent with antityrosinase effect. Moracinoside M (4) and moracin M-3'-O-${\beta}$-D-glucopyranoside (5) also showed the moderate tyrosinase inhibitory activities.

Keywords

References

  1. Jeong, S.H., Ryu, Y.B., Curtis-Long, M.J., Ryu, H.W., Baek, Y.S., Kang, J.E., Lee, W.S., and Park, K.H., Tyrosinase inhibitory polyphenols from roots of Morus Ihou. J. Agric. Food Chem., 57, 1195-1203 (2009). https://doi.org/10.1021/jf8033286
  2. Kanchanapoom, T., Suga, K., Kasai, R., Yamasaki, K., Kamel, M. S., and Mohamed, M. H., Stilbene and 2-Arylbenzofuran Glucosides from the Rhizomes of Schoenocaulon officinale. Chem. Pharm. Bull., 50, 863-865 (2002). https://doi.org/10.1248/cpb.50.863
  3. Katib, S., Nerya, O., Musa, R., Shmuel, M., Tamir, S., and Vaya, J., Chalcones as potent tyrosinase inhibitors : the importance of a 2, 4-substituted resorcinol moiety. Bioorg. Med. Chem., 13, 433-441 (2005). https://doi.org/10.1016/j.bmc.2004.10.010
  4. Lee, S.H., Choi, S.Y., Kim, H.C., Hwang, J.S., Lee, B.G., Gao, J.J., and Kim, S.Y., Mulberroside F isolated from the leaves of Morus alba inhibits melanin biosynthesis. Biol. Pharm. Bull., 25, 1045-1048 (2002). https://doi.org/10.1248/bpb.25.1045
  5. Lim, S.S., Jung S.H., Ji, J., Shin, K.H., and Keum, S.R., Synthesis of flavonoids and their effect on aldose reductase and sorbitol accumulation in streptozotocin-induced diabetic rat tissues. J. Pharm. Pharmacol., 53, 653-668 (2001). https://doi.org/10.1211/0022357011775983
  6. Martinez-Esparza, M., Jimenez-Cervantes, C., Solano, F., Lozano, J.A., and Garcia-Borron, J.C., Mechanisms of melanogenesis inhibition by tumor necrosis factor-alpha in B16/F10 mouse melanoma cells. Eur. J. Biochem, 255, 139-146 (1998). https://doi.org/10.1046/j.1432-1327.1998.2550139.x
  7. Mayer, A.M., Polyphenol oxidases in plants: recent progress. Phytochemistry, 26, 11-20 (1987).
  8. Nerya, O., Musa, R., Khatib, S., Tamir, S., and Vaya, J., Chalcones as potent tyrosinase inhibitors : the effect of hydroxyl positions and numbers. Phytochemistry, 65, 1389-1395 (2004). https://doi.org/10.1016/j.phytochem.2004.04.016
  9. Shin, N.H., Ryu, S.Y., Choi, E.J., Kang, S.H., Chang, I.M., Min, K.R., and Ki, Y.S., Oxyresveratrol as the potent inhibitor on Dopa oxidase activity of mushroom tyrosinase. Biochem Biophys Res Commun., 243, 801-803 (1998). https://doi.org/10.1006/bbrc.1998.8169
  10. Siegbahn, P.E., A comparison of the thermodynamics of O-O bond cleavage for dicoppor complexes in enzymes and synthetic systems. J. Biol. Inorg. Chem., 8, 577-585 (2003). https://doi.org/10.1007/s00775-003-0451-x
  11. Slominski, A., Tobin, D.J., Shibahara, S., and Wortman, J., Melanin pigmentation in mammalian skin and its hormonal regulation. Phys. Rev. 84, 1155-1228 (2004). https://doi.org/10.1152/physrev.00044.2003
  12. Solano, F., Briganti, S., Picardo, M., and Ghanem, G., Hypopigmenting agents : an updated review on biological, chemical and clinical aspects. Pigment Cell Res., 19, 550-571 (2006). https://doi.org/10.1111/j.1600-0749.2006.00334.x
  13. Van Gelder, C.W., Flurkey, W.H., and Wichers, H.J., Sequence and structural features ofplantand fungal tyrosinases. Phytochemistry, 45, 1309-1323 (1997). https://doi.org/10.1016/S0031-9422(97)00186-6