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Year : 2013  |  Volume : 2  |  Issue : 2  |  Page : 156-164

Kinetic of mushroom tyrosinase inhibition by benzaldehyde derivatives

1 Medical Biology Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran
2 Novel Drug Delivery Research Center, Faculty of Pharmacy, Kermanshah University of Medical Sciences, Kermanshah, Iran
3 Proteomics Research Center, Faculty of Paramedical Sciences, Shahid-Beheshti University of Medical Sciences, Tehran, Iran

Correspondence Address:
Reza Khodarahmi
Medical Biology Research Center, Kermanshah University of Medical Sciences, Kermanshah
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Source of Support: None, Conflict of Interest: None

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Polyphenol oxidase (PPO), known as tyrosinase (EC, is a multifunctional copper-containing oxidase which catalyzes the rate-limiting step in the formation of melanin from tyrosine. This enzyme is responsible not only for enzymatic browning in plants but also for melanogenesis in mammals. Thus, tyrosinase inhibitors have a huge impact on industry and the economy. In the current study, at first the enzyme was purified and then we evaluated inhibitory potency of three benzaldehyde derivatives: 2,4-dihydroxybenzaldehyde, 3,4-dihydroxybenzaldehyde and 4-dimethylaminobenzaldehyde on diphenolase activity of the purified mushroom tyrosinase, compared to kojic acid. Despite their close structural similarity, 2,4-dihydroxybenzaldehyde was found as a potent and competitive inhibitor while a weak uncompetitive inhibition was observed for 4-dimethylaminobenzaldehyde. Further complementary studies on these types of inhibitors, as potential drug candidates for treating abnormal melanin pigmentation, are needed.

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