Antifreeze peptides from Antarctic yeast Glaciozyma antarctica for enhanced cell cryopreservation

The Antarctic yeast Glaciozyma antarctica isolated near the Casey Station, Antarctica produces a novel antifreeze protein (AFP) with a very low (<20%) homologous sequence to other AFP, of which several antifreeze peptides (Afp) were predicted ab initio based on α-helical sequences. Four patented Afp peptides were customised and synthesised using solid-phase peptide methods. All Afp structures were confirmed by nuclear magnetic resonance (NMR), revealing their helical structures and flexibility. Molecular dynamics simulations of Afp and ice crystals revealed the binding of selected amino acids to the ice, mimicking the antifreeze mechanism. These non-allergenic “ice-structuring peptides” show high antifreeze activity and inhibit recrystallisation. Pre-cryopreservation cytotoxicity, histological and mechanical evaluation of cryopreserved skin grafts with Afp1m after transplantation in a rat model showed low toxicity and rapid recovery. Antifreeze peptides can be produced cost-effectively in large quantities and are used to improve food texture, cryopreserve organs, and the long-term storage of biological material such as sperm, embryos, and blood cells.

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