期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 63, 期 27, 页码 6181-6188出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.5b01026
关键词
tyrosinase; peptide; melanin; molecular docking eumelanin formation; dopachrome
资金
- National Research Institute of Chinese Medicine, Ministry of Health and Welfare [MM10211-0153, MM10401-0394]
- Ministry of Science and Technology, Taipei, Taiwan [MOST 103-2320-B-077-001-MY3]
Tyrosinase is an essential copper-containing enzyme required for melanin synthesis. The overproduction and abnormal accumulation of melanin cause hyperpigmentation and neurodegenerative diseases. Thus, tyrosinase is promising for use in medicine and cosmetics. Our previous study identified a natural product, AS, resembling the structure of the dipeptide WY and apparently inhibiting tyrosinase. Here, we comprehensively estimated the inhibitory capability of 20 X 20 dipeptides against mushroom tyrosinase. We found that cysteine-containing dipeptides, directly blocking the active site of tyrosinase, are highly patent in inhibition; in particular, N-terminal cysteine-containing dipeptides markedly outperform the C-terminal-containing ones. The cysteine-containing dipeptides, CE; CS, CY, and CW, show comparative bioactivities, and tyrosine-containing dipeptides are substrate-like inhibitors. The dipeptide PD attenuates 16.5% melanin content without any significant cytotoxicity. This study reveals the functional role of cysteine residue positional preference and the selectivity of specific amino acids in cysteine-containing dipeptides against tyrosinase, aiding in developing skin-whitening products.
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