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The Hypopigmentation Mechanism of Tyrosinase Inhibitory Peptides Derived from Food Proteins: An Overview

文献类型: 外文期刊

作者: Song, Yuqiong 1 ; Chen, Shengjun 1 ; Li, Laihao 1 ; Zeng, Yaoxun 4 ; Hu, Xiao 1 ;

作者机构: 1.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Key Lab Aquat Prod Proc, Minist Agr & Rural Affairs, Guangzhou 510300, Peoples R China

2.Jiangsu Ocean Univ, Coinnovat Ctr Jiangsu Marine Bioind Technol, Lianyungang 222005, Peoples R China

3.Shanghai Ocean Univ, Coll Food Sci & Technol, Shanghai 201306, Peoples R China

4.Guangdong Univ Technol, Sch Biomed & Pharmaceut Sci, Guangzhou 510006, Peoples R China

5.Dalian Polytech Univ, Collaborat Innovat Ctr Prov & Ministerial Coconst, Dalian 116034, Peoples R China

关键词: bioactive peptides; tyrosinase activity; hyperpigmentation; mechanism; molecular docking

期刊名称:MOLECULES ( 影响因子:4.927; 五年影响因子:5.11 )

ISSN:

年卷期: 2022 年 27 卷 9 期

页码:

收录情况: SCI

摘要: Skin hyperpigmentation resulting from excessive tyrosinase expression has long been a problem for beauty lovers, which has not yet been completely solved. Although researchers are working on finding effective tyrosinase inhibitors, most of them are restricted, due to cell mutation and cytotoxicity. Therefore, functional foods are developing rapidly for their good biocompatibility. Food-derived peptides have been proven to display excellent anti-tyrosinase activity, and the mechanisms involved mainly include inhibition of oxidation, occupation of tyrosinase's bioactive site and regulation of related gene expression. For anti-oxidation, peptides can interrupt the oxidative reactions catalyzed by tyrosinase or activate an enzyme system, including SOD, CAT, and GSH-Px to scavenge free radicals that stimulate tyrosinase. In addition, researchers predict that peptides probably occupy the site of the substrate by chelating with copper ions or combining with surrounding amino acid residues, ultimately inhibiting the catalytic activity of tyrosinase. More importantly, peptides reduce the tyrosinase expression content, primarily through the cAMP/PKA/CREB pathway, with PI3K/AKT/GSK3 beta, MEK/ERK/MITF and p38 MAPK/CREB/MITF as side pathways. The objective of this overview is to recap three main mechanisms for peptides to inhibit tyrosinase and the emerging bioinformatic technologies used in developing new inhibitors.

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