Ph.D. student at Prof. Ido Braslavsky’s labInvestigation of Ice Binding Proteins Applications for Cryopreservation of Biological Systems
Meeting ID: 837 9858 8498, Passcode: 217555
Ice binding proteins (IBPs) have evolved in various organisms to permit their survival in cold environments. They possess unique properties such as freezing point depression (antifreeze proteins, AFPs) and ice recrystallization inhibition. These properties grant them the potential to be used in cryopreservation (e.g., slow freezing and vitrification) of biological systems. In slow freezing cells, suspensions are cooled at -1 °C/min and then stored at −196 °C. In vitrification, an ultrafast cooling rate down to −196 °C combined with the addition of a high concentration of cryoprotectants is applied to achieve an amorphous glass state in the absence of crystallization. Ice growth and recrystallization occur during the warming of vitrified solutions, a process termed devitrification and is harmful to cryopreserved biological material. This research investigates the function of two types of AFPs (type III AFP and MBP-TmAFP) as low toxicity cryoprotective agents and their effectiveness in inhibition of devitrification and ice recrystallization during the warming of vitrified solutions.