Copper chelating peptides derived from tilapia (Oreochromis niloticus) skin as tyrosinase inhibitor: Biological evaluation, in silico investigation and in vivo effects

Yuqiong Song; Jun Li; Han Tian; Huan Xiang; Shengjun Chen; Laihao Li; Xiao Hu

doi:10.1016/j.foodres.2022.112307

Copper chelating peptides derived from tilapia (Oreochromis niloticus) skin as tyrosinase inhibitor: Biological evaluation, in silico investigation and in vivo effects

Food Res Int. 2023 Jan:163:112307. doi: 10.1016/j.foodres.2022.112307. Epub 2022 Dec 8.

Authors

Yuqiong Song¹, Jun Li², Han Tian³, Huan Xiang⁴, Shengjun Chen⁴, Laihao Li⁴, Xiao Hu⁵

Affiliations

¹ Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China.
² CAS Key Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Key Laboratory of Marine Materia Medica, RNAM Center for Marine Microbiology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou 510301, China. Electronic address: [email protected].
³ College of Marine Sciences, Shanghai Ocean University, Shanghai 201306, China.
⁴ Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China; Co-Innovation Center of Jiangsu Marine Bio-Industry Technology, Jiangsu Ocean University, Lianyungang 222005, China.
⁵ Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China; Co-Innovation Center of Jiangsu Marine Bio-Industry Technology, Jiangsu Ocean University, Lianyungang 222005, China; Collaborative Innovation Center of Provincial and Ministerial Co-Construction for Marine Food Deep Processing, Dalian Polytechnic University, Dalian 116034, China. Electronic address: [email protected].

PMID: 36596203
DOI: 10.1016/j.foodres.2022.112307

Abstract

Binuclear copper ions at the active site determine the catalysis of tyrosinase (TYR)¹ whose activity can be inhibited by copper's chelation with other compounds. In this study, tilapia (Oreochromis niloticus) skin was used to generate TYR-inhibitory peptides after being treated by different enzymes and 4 h-Alcaline protease hydrolysate exhibited the highest TYR inhibition and copper chelation. Immobilized metal affinity chromatography was used for purifying copper chelating peptides, among which PFRMY (IC₅₀: 0.43 ± 0.08 mg/mL) and RGFTGM (IC₅₀: 1.61 ± 0.04 mg/mL) exhibited the highest TYR-inhibitory capacity and the lowest docking energy. Both two peptides inhibited TYR in a mixed manner and interacted with key residues binding to copper ions within TYR mainly by hydrogen bonds and hydrophobic forces, while PFRMY had a more compact and stable conjugation with TYR. Zebrafish assay revealed that PFRMY reduced not only melanin synthesis but in vivo TYR activity.

Keywords: Copper chelating peptides; Molecular dynamics; Tilapia (Oreochromis niloticus) skin; Tyrosinase inhibition.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Cichlids* / metabolism
Copper
Ions
Monophenol Monooxygenase
Peptides / chemistry
Peptides / pharmacology
Tilapia* / metabolism
Zebrafish / metabolism

Substances

Monophenol Monooxygenase
Copper
Peptides
Ions