Divergent Mechanisms of Ice Growth Inhibition by Antifreeze Proteins

Antifreeze proteins (AFPs) are biomolecules that can bind to ice and hinder its growth, thus holding significant potential for biotechnological and biomedical applications. AFPs are a subset of ice-binding proteins (IBPs) and are found in various organisms across different life kingdoms. This mini-review investigates the underlying mechanisms by which AFPs impede ice growth, emphasizing the disparities between hyperactive and moderate AFPs. Hyperactive AFPs exhibit heightened thermal hysteresis (TH) activity and can bind to both the basal and prism planes of ice crystals, enabling them to endure extremely cold temperatures. In contrast, moderate AFPs predominantly bind to the prism/pyramidal planes and demonstrate lower TH activity. The structural diversity of AFPs and the presence of ordered water molecules on their ice-binding sites (IBS) have been subjects of debate among researchers. Multiple hypotheses have been proposed concerning the significance of ordered water molecules in ice binding. Gaining insights into the binding dynamics and the factors influencing TH activity in AFPs is crucial for the development of efficient synthetic compounds and the establishment of comprehensive models to elucidate ice growth inhibition. Here we emphasize the necessity for further research to unravel the mechanisms of AFPs and presents a pathway for constructing models capable of comprehensively explaining their inhibitory effects on ice growth.