Several organisms have evolved specialized ice binding proteins (IBPs) that prevent their body fluids from freezing (antifreeze proteins, AFPs), inhibit recrystallization of ice in frozen tissues, or initiate freezing at moderate supercooling temperatures (ice nucleating proteins, INPs). These proteins have many potential applications in agriculture, food preservation, cryobiology, and biomedical science. The ubiquitous presence of IBPs in such organisms indicates the power of these molecules to enable survival under cold conditions. Despite this key role in nature, however, IBPs have been effectively exploited in only one cryopreservation application, namely, recrystallization inhibition in ice cream. Several terrestrial organisms, including insects, have developed very active forms of AFPs. These hyperactive AFPs (hypAFPs) have not been utilized significantly thus far in cryopreservation techniques. The gap between the obvious potential of IBPs and their actual applications stems from a lack of knowledge regarding the mechanisms by which IBPs interact with ice surfaces and how these proteins can assist in cryoprotection. I propose to investigate the mechanism by which IBPs inhibit ice crystallization and the use of such proteins for cryopreserving cells, tissues, and organisms. My group has a strong record in the study of the interactions between IBPs and ice using novel methods that we have developed, including fluorescence microscopy techniques combined with cooled microfluidic devices. We will investigate the interactions of AFPs with ice and the use of hypAFPs in cryopreservation procedures. This research will contribute to an understanding of the mechanisms by which IBPs act, and apply the acquired knowledge to cryopreservation. The successful implementation of IBPs in cryopreservation would revolutionize the field of cryobiology, with enormous implications for cryopreservation applications in general and the frozen and chilled food industry in particular.
Call for proposal
See other projects for this call