A novel supramolecular cryopreservation nanoagent based on self-assembly of peptide

Abstract

Cryopreservation is very important in biotechnological, pharmaceutical, biochemical or food industries as the purpose of storage of protein drugs, cells, tissues and food, and ice slurries for refrigeration systems. Antifreeze protein (AFP) have been received attention with their potential as a cryopreservation agent by their ability to prevent the organisms from freezing at the subzero environment through antifreeze activity such as ice recrystallization inhibition or thermal hysteresis effect. However, it is struggling to apply the natural AFP in practical industries as cryopreservation agent because of their irreversible denaturation and the difficulty in extraction from nature. These challenges have led to developing artificial cryopreservation agents like dimethyl sulfoxide and sodium phosphates but due to the cytotoxicity and less biocompatible of them, the recovery rate of the target matter is too low when they are added. Here, the natural AFP mimetic short peptides conjugated with specific amino acids showing antifreeze activity and fibrous assembly with enhanced π-π stacking are prepared by supramolecular chemistry to increase both antifreeze activity and biocompatibility. This research might provide a useful strategy to fabricate the cryopreservation agent through the supramolecular nanomaterials and to figure out the mechanism of ice binding to antifreeze protein.