Supramolecular antifreezing peptide nanoagents for cellular cryopreservation

Abstract

Cryopreservation is critical factor in a fields of biochemical, pharmaceutical, biotechnological, and food industries, when it comes to storing cells, tissues, proteins, drugs, and foods. Antifreeze proteins (AFPs) have attracted huge interest with their cryopreservation activity originated from ice recrystallization inhibition or thermal hysteresis effects, which prevents organisms from freezing at the subzero environment. It is still challenging to develop new cryoprotectants mimicking natural AFPs for practical use due to the lack of understanding of structure-antifreezing activity relationship. The commercially available antifreezing agents show potential cytotoxicity to be applied for a biomedical field. Here, the self-assembled peptide nanoagents mimicking the AFPs were rationally designed by supramolecular chemistry to enhance both antifreeze activity and biocompatibility. The various nanostructures of the peptide nanoagents, changed by the hydrophobicity and hydrophilicity of periodically arranged antifreezing moieties, affect ice binding and resultant ice growth inhibition. Then it was confirmed that the survive rate of frozen-thawed stem and germ cells were increased after cryopreservation of peptide nanoagents and the revitalization of them were evaluated. This research could provide a useful strategy for manufacturing a cryopreservation agents with high performance through supramolecular chemistry and figuring out the mechanism of how AFPs affects cellular cryopreservation.