Abstract

Antifreeze proteins and ice-binding proteins have been discovered in a diverse range of extremophiles and have the ability to modulate the growth and formation of ice crystals. Considering the importance of cryoscience across transport, biomedicine, and climate science, there is significant interest in developing synthetic macromolecular mimics of antifreeze proteins, in particular to reproduce their property of ice recrystallization inhibition (IRI). This activity is a continuum rather than an “on/off” property and there may be multiple molecular mechanisms which give rise to differences in this observable property; the limiting concentrations for ice growth vary by more than a thousand between an antifreeze glycoprotein and poly(vinyl alcohol), for example. The aim of this article is to provide a concise comparison of a range of natural and synthetic materials that are known to have IRI, thus providing a guide to see if a new synthetic mimic is active or not, including emerging materials which are comparatively weak compared to antifreeze proteins, but may have technological importance. The link between activity and the mechanisms involving either ice binding or amphiphilicity is discussed and known materials assigned into classes based on this.

Highlights

  • Antifreeze proteins and ice-binding proteins have been discovered in a reviewed.[1,2,3,4] The ability to modulate ice diverse range of extremophiles and have the ability to modulate the growth formation and growth has vast technologand formation of ice crystals

  • Introduction main properties resulting from their ice interactions; non-colligative depression of the freezing point (thermal hysteresis (TH)), Antifreeze, ice-binding and ice-nucleating macromolecules dynamic ice shaping (DIS); ice recrystallization inhibition (IRI) activity

  • The latter (IRI) is of parhave been discovered in a diverse range of extremophile organ- ticular interest, as it was discovered in 2003 that synthetic mimics isms from fish to insects to plants

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Summary

Measuring IRI Activity

The first, and most widely used, method for measuring IRI is the “splat” assay as shown by Knight.[26] This assay enables quick assessment of IRI activity by monitoring the growth of ice grains that have been nucleated rapidly at low temperatures (≈−80 °C) to ensure only growth (not nucleation) events are probed This is a kinetic assay, shorter time points will always give smaller crystals. Professor Gibson’s multidisciplinary research group focusses on developing biomaterials to address healthcare challenges including pathogen detection/neutralization with glycomimetics and new technologies for the storage and transport of biologics, inspired by extremophile biology This article contains both new, and previously published IRI activity, focusing on that obtained by the “splat” assay where possible to allow critical comparison

Proteins and Polymers Which Bind Ice
Ice-Binding Self-Assembled Materials
Flexible Polymers and Hydrophobicity
Summary
Conclusions
Experimental Section
Findings
Conflict of Interest

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