IBPs-mimicking nanocryoprotectants for ice-water interface control
발표자
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초록
내용
Ice-binding proteins (IBPs) play a crucial role in the cryopreservation of drugs, cells, tissues, and foods with their thermal hysteresis and ice recrystallization inhibition activity. Artificial cryoprotectants mimicking IBP structure and function have been developed to prevent cryo-damage, but existing organic ones are easily deformed, and inorganic ones are cytotoxic. In this regard, organic-inorganic nanohybrids are in demand. We studied the effect of thermodynamics on the performance of nanohybrids composed of ice-binding short-peptides and inorganic nanoparticles (NPs) by controlling the interaction with the ice-water interface. The interactions were controlled by aligning the organic ice-binding moieties on the ice lattice or by controlling the colloid size and directly imaged using the tethered-NPs. The optimal conditions for thermodynamically controlling the interface were explored, providing a strategy for practical cellular cryopreservation, organ transplantation, cord blood storage, and vaccines/drugs.