Unraveling the Cryoprotective Molecular Mechanisms of Antifreeze Peptides: New Insights from Simultaneous Interactions with Ice Crystals and Lactalbumin Proteins

. Differential scanning calorimetry indicated that GKEAFP, GLPAFP, and GLRAFP most effectively inhibited ice growth. Molecular docking demonstrated stable peptide-ice and peptide-α-lactalbumin interactions, with GLPAFP notably stabilizing protein structures through extensive hydrogen bonding and surface interactions. These findings suggest that gelatin-derived antifreeze peptides suppress ice recrystallization and stabilize proteins via amphiphilic ice-binding motifs, providing promising natural cryoprotectants for frozen food applications.