A systematic review of synthetic tyrosinase inhibitors and their structure-activity relationship

Tyrosinase is a copper-containing oxidation enzyme, which is responsible for the production of melanin. This enzyme is widely distributed in microorganisms, animals and plants, and plays an essential role in undesirable browning of fruits and vegetables, antibiotic resistance, skin pigment formation...

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Published in:Critical reviews in food science and nutrition 2022, Vol.62 (15), p.4053-4094
Main Authors: Peng, Zhiyun, Wang, Guangcheng, Zeng, Qiao-Hui, Li, Yufeng, Liu, Haiquan, Wang, Jing Jing, Zhao, Yong
Format: Article
Language:English
Subjects:
Antibacterial agents
Antibiotic resistance
Antibiotics
Antiinfectives and antibacterials
Chemical compounds
Cytotoxicity
Enzymes
Inhibitors
Insecticide resistance
Insecticides
Melanin
Microorganisms
molecular docking
Neurodegeneration
Oxidation
Pharmaceutical industry
Pharmacology
Sclerotization
Skin
Skin resistance
structure-activity relationship
synthetic compounds
Therapeutic targets
Toxicity
Tyrosinase
Tyrosinase inhibitors
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Summary:Tyrosinase is a copper-containing oxidation enzyme, which is responsible for the production of melanin. This enzyme is widely distributed in microorganisms, animals and plants, and plays an essential role in undesirable browning of fruits and vegetables, antibiotic resistance, skin pigment formation, sclerotization of cuticle, neurodegeneration, etc. Hence, it has been recognized as a therapeutic target for the development of antibrowning agents, antibacterial agents, skin-whitening agents, insecticides, and other therapeutic agents. With great potential application in food, agricultural, cosmetic and pharmaceutical industries, a large number of synthetic tyrosinase inhibitors have been widely reported in recent years. In this review, we systematically summarized the advances of synthetic tyrosinase inhibitors in the literatures, including their inhibitory activity, cytotoxicity, structure-activity relationship (SAR), inhibition kinetics, and interaction mechanisms with the enzyme. The collected information is expected to provide a rational guidance and effective strategy to develop novel, potent and safe tyrosinase inhibitors for better practical applications in the future.
ISSN:1040-8398
1549-7852
DOI:10.1080/10408398.2021.1871724