Abstract
The color of mammalian skin is determined by many factors, for which visible ones are the degree and distribution of melanin pigmentation. Because tyrosinase, (polyphenol oxidase) is the key enzyme for melanin biosynthesis, the use of various tyrosinase inhibitors is a common practice for whitening purpose in cosmetics. In the present study, the inhibition of tyrosinase by 4,4'-dihydroxybiphenyl (44'-BP) was investigated. In addition to tyrosinase inhibiting activity, melanin biosynthesis was assessed in B16F10 melanoma cells (B16 cells). The results showed that 44'-BP exhibits a strong anti-tyrosinase activity with IC50=1.91 microM. The kinetic analysis of tyrosinase inhibition revealed that 44'-BP acts a competitive inhibitor (Ki=4.0 x 10(-4) M at 2.5 microM and Ki =21 x 10(-5) M at 5 microM). Furthermore, data on melanin biosynthesis indicated that the amount of melanin was clearly suppressed by 44'-BP.
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