Identification of Novel Antifreeze Peptides from Takifugu obscurus Skin and Molecular Mechanism in Inhibiting Ice Crystal Growth

• Published in: Journal of agricultural and food chemistry Vol. 70; no. 44; pp. 14148 - 14156
• Main Authors: Yang, Fujia, Jiang, Wenting, Chen, Xu, Chen, Xuan, Wu, Jinhong, Huang, Jianlian, Cai, Xixi, Wang, Shaoyun
• Format: Journal Article
• Language: English
• Published: American Chemical Society 09.11.2022
• Subjects: Bioactive Constituents, Metabolites, and Functions; antifreeze mechanism; sequence screening; antifreeze peptides; identification; molecular docking
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/acs.jafc.2c04393

Foodborne hydrolyzed antifreeze peptides have been widely used in the food industry and the biomedical field. However, the components of hydrolyzed peptides are complex and the molecular mechanism remains unclear. This study focused on identification and mechanism analysis of novel antifreeze peptides from Takifugu obscurus skin by traditional methods and computer-assisted techniques. Results showed that three peptides (EGP­RAG­GAPG, GDA­GPS­GPA­GPTG, and GEA­GPA­GPAG) possessed cryoprotection via reducing the freezing point and inhibiting ice crystal growth. Molecular docking confirmed that the cryoprotective property was related to peptide structure, especially α-helix, and hydrogen bond sites. Moreover, the antifreeze peptides were double-faces, which controlled ice crystals while affecting the arrangement of surrounding water molecules, thus exhibiting a strong antifreeze activity. This investigation deepens the comprehension of the mechanism of antifreeze peptides at molecular scale, and the novel efficient antifreeze peptides can be developed in antifreeze materials design and applied in food industry.