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.