Abstract
Antifreeze proteins (AFPs), occurring in some polar animals, plants, fungi, and other organisms, are capable of inhibiting ice freezing at subzero temperatures. The application of AFPs can be found in medicine and industry where low temperature storage is required and ice crystallization is damaging. This includes improved protection of blood platelets and human organs at low temperature, increasing the effectiveness of the destruction of malignant tumors in cryosurgery, and improvement of the smooth texture of frozen foods. In this review, the antifreeze mechanisms of AFPs are discussed, focusing on their inhibition effects on both ice nucleation and crystal growth. AFPs have been found to act in two stages. As a precursor to ice growth, ice nucleation is suppressed by the surface adsorption of AFPs to both ice nucleus and ice nucleators. At the second stage, in cases where inhibition of ice nucleation has had partial or no success, AFPs proceed to inhibit the growth of ice by adsorbing on specific surfaces of ice. Based on the understanding of structure–activity relationship, one is able to mimic the active domain of AFGPs and synthesize antifreeze glycoproteins by using ligation and polymerization strategies. However, further optimization of the chemistry, as well as new routes to mimic AFPs and functional analogues are needed to allow the routine production of quantities of pure material on commercially relevant scales.
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Du, N., Toh, G.W., Liu, X.Y. (2012). Survival from the Cold Winter: Freezing and Ice Crystallization Inhibition by Antifreeze Proteins. In: Liu, X. (eds) Bioinspiration. Biological and Medical Physics, Biomedical Engineering. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-5372-7_2
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