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

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 alpha-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.

Automated summary

This study identified novel antifreeze peptides from Takifugu obscurus skin and confirmed their cryoprotective properties through traditional methods and computer assisted techniques. Molecular docking showed that the cryoprotective property was related to peptide structure, especially alpha-helix, and hydrogen bond sites. The antifreeze peptides controlled ice crystals and affected surrounding water molecules, exhibiting strong antifreeze activity. This research deepens the understanding of antifreeze peptides at molecular scale and their potential applications in antifreeze materials design and food industry.