| RESEARCH ARTICLE |
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| Year : 2013 | Volume
: 2
| Issue : 2 | Page : 156-164 |
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Kinetic of mushroom tyrosinase inhibition by benzaldehyde derivatives
Shabnam Maghsoudi1, Hadi Adibi2, Marzieh Hamzeh2, Mohammad Reza Ashrafi-Kooshk1, Mostafa Rezaei-Tavirani3, Reza Khodarahmi1
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
Iran
 Source of Support: None, Conflict of Interest: None  | Check |
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Polyphenol oxidase (PPO), known as tyrosinase (EC 1.14.18.1), 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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