Downsizing antifreeze proteins to antifreeze peptides from Antarctica inhabitants

S cold-adapted organisms are able to synthesize antifreeze protein (AFP) to enable them to survive in subzero environment. The ability of AFP to reduce the ice damage in cells has attracted interest in many applications for example medical and agriculture sectors. However, high capital cost in producing AFP may hamper them to be resourcefully used in industrial biotechnology. Lately, peptides that mimic the parent proteins have been designed and synthesized for many purposes. AFP type I from Antarctic yeast Glaciozyma antarctica and shorthorn sculpin fish, Myoxocephalus scorpius were downsized to functional several α-helix antifreeze peptides. The short peptide segments derived from both AFPs gave high antifreeze activity and ice recrystallization inhibition. Molecular modeling ofα-helix antifreeze peptides on ice surface showed the straightforwardness of the peptides is related to the high antifreeze activity. These synthetic antifreeze peptides could be a new hope in food preservation and cryopreservation technology as it could inhibit the growth of ice crystals.