Mushroom Tyrosinase Inhibition Activity of Some Chromones.

Piao, Long Zhu; Park, Hyang Rae; Park, Yun Kyung; Lee, Seung Ki; Park, Jeong Hill; Park, Man Ki

doi:10.1002/chin.200235134

Cited by 7 publications

(7 citation statements)

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“…Tyrosinase inhibition activity was determined in vitro using L-tyrosine as the substrate using a modified method from Piao et al (2002). The concentration of enzyme, substrate, and inhibitor was denoted as [E], [S], and [I], respectively.…”

Section: Enzymatic Assay Of Mushroom Tyrosinasementioning

confidence: 99%

Short-Sequence Oligopeptides with Inhibitory Activity against Mushroom and Human Tyrosinase

Ubeid

Zhao

Wang

et al. 2009

Journal of Investigative Dermatology

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Cutaneous hyperpigmentation is a common disorder due to excess melanin production by the enzyme tyrosinase. The gold standard for treatment is hydroquinone (HQ), which reduces pigmentation through its toxicity to melanocytes rather than via tyrosinase inhibition. We screened an internal library for oligopeptides that inhibited both mushroom and human tyrosinase but showed no cytotoxicity to human melanocytes. We identified two highly active inhibitory sequences, P3 and P4, of 8- and 10-amino-acid-length, respectively. Mushroom tyrosinase inhibition was dose-dependent with IC(50) (half-maximal inhibitory concentration) values of 123 and 40 microM, respectively, compared with 680 microM for HQ. Other oligopeptides showed weaker or no inhibitory activity. Kinetic studies showed that P3 and P4 are competitive inhibitors of mushroom tyrosinase. At 100 microM, P3 and P4 inhibited human tyrosinase by 25-35%. This inhibition partially depended on whether L-dopa or L-tyrosine was the substrate, suggesting that tyrosinase may contain contains two distinct catalytic sites. Treatment of melanocytes with 100 microM P3 or P4 for 7 days led to a 27 or 43% reduction in melanin content. This inhibition was independent of cell proliferation and cytotoxic effects. Our data suggest that peptide-mediated inhibition of melanogenesis is due to reduction in tyrosinase activity.

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Section: Enzymatic Assay Of Mushroom Tyrosinasementioning

confidence: 99%

Short-Sequence Oligopeptides with Inhibitory Activity against Mushroom and Human Tyrosinase

Ubeid

Zhao

Wang

et al. 2009

Journal of Investigative Dermatology

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“…5-Methyl-7-methoxy-2-(2'-benzyl-3'-oxobutyl)chromone exhibited the strongest activity, and higher than the reference (IC 50 0.03 and 0.09 mM for kojic acid, respectively). According to kinetic analysis, it is a competitive inhibitor with TYR for the L-tyrosine binding site [11]. No activity was observed for cimifugin in the present assays.…”

mentioning

confidence: 50%

Development of an Efficient Protocol for Cimifugin Isolation from Peucedanum schottii and Evaluation of Enzyme Inhibitory Activity

Kozioł

et al. 2016

Natural Product Communications

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The dichloromethane (DCM) extract of the fruits of Peucedanum schottii Besser ex DC. (Apiaceae) was subjected to high-performance counter-current chromatography (HPCCC) for the efficient and fast separation (30 min) and isolation of cimifugin using an ethyl acetate: water (1:1 v/v, K = 1.01) system. The analytical scale-optimized separation was easily scaled to semi-preparative conditions. Cimifugin (11.25% yield, 96.5% purity) was isolated for the first time from P. schottii and characterized by NMR spectroscopy. Cimifugin and the crude DCM extract were evaluated using ELISA microtiter assays for their inhibitory potential against the cholinesterases (acetylcholinesterase - AChE and butyrylcholinesterase - BChE), and tyrosinase (TYR), which are key enzymes for the treatment of some neurodegenerative diseases, i.e. Alzheimer's and Parkinson's. The crude extract exhibited a weak inhibitory activity against AChE, BChE, and TYR (4.2, 35.5, and 0% at 100 μg mL−1 and 10.3, 40.0, and 12.2% at 200 μg mL−1, respectively), while cimifugin displayed low to moderate inhibition towards AChE and BChE (3.1 and 21.6%, respectively) at 200 μg mL−1.

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“…In cultured normal melanocytes, aloesin inhibits melanin production 115 . Aloesin has been shown to be an even stronger tyrosinase inhibitor than arbutin and kojic acid 116 . When administered four times a day for 15 days for hyperpigmentation in human skin after UV radiation, aloesin reduced pigmentation by 34% in a dose‐dependent manner; the combination of aloesin and arbutin diminished pigmentation by 63.3% compared with the control 117 …”

Section: Botanicalsmentioning

confidence: 99%