Do antifreeze proteins generally possess the potential to promote ice growth?

Cui, Shaoli; Zhang, Weijia; Shao, Xueguang; Cai, Wensheng

doi:10.1039/d1cp05431g

Cited by 8 publications

(4 citation statements)

References 64 publications

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“…51 This damage results in part from the 10% expansion as liquid water becomes ice; the larger volume of ice causes cells to burst. One model for protection is to generate a critical concentration of protein in the extracellular fluid that both induces the formation of nanoscopic ice crystallites 52 and inhibits the growth of larger crystals. 53,54 Within this picture, the protein has both an iceface templating region and typically a more hydrophobic region.…”

Section: Ice−water Interfacementioning

confidence: 99%

“…This damage results in part from the 10% expansion as liquid water becomes ice; the larger volume of ice causes cells to burst. One model for protection is to generate a critical concentration of protein in the extracellular fluid that both induces the formation of nanoscopic ice crystallites and inhibits the growth of larger crystals. , Within this picture, the protein has both an ice-face templating region and typically a more hydrophobic region. − The splat assay builds on this idea, measuring inhibition by dropping water droplets onto a cold substrate (typically about −80 °C), thereby generating a large number of small crystallites due to flash freezing the sample, warming the resulting polycrystalline sample to a subzero temperature (−8 °C is typical), and holding the sample at this annealing temperature for a prescribed period. Consistent with a model of limiting ice crystallite size, splat assay analysis consists of either counting the number of crystals or measuring the morphology of the surviving crystals .…”

Section: Ice–water Interfacementioning

confidence: 99%

“…Growth at the ice–water interface is of interest in fields ranging from cloud seeding , to organ preservation to ice prevention on airplanes . As discussed above, experimentally probing growth at the ice–water interface is challenging, a challenge made even greater if the goal is to probe the impact of solution additives to build a molecular model for effective ice-growth modifiers. ,,− At the present time, the most common assays are the splat assay and the sucrose sandwich assay . The common thread connecting these two assays is measuring the average crystallite size/number.…”

Section: Ice–water Interfacementioning

confidence: 99%

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Ice Interfaces: Vapor, Liquid, and Solutions

Shultz,

Gubbins,

Davies

et al. 2024

J. Phys. Chem. C

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Interfaces between hexagonal ice and its vapor, liquid water, and aqueous solutions are all of central importance to life on earth. Despite its importance, much remains unknown about the ice interface, particularly at the molecular level. This contribution contains a brief survey of these three interfaces, emphasizing experimental results. Remarkably, evidence suggests that the secondary prism face is the most stable face at both the ice−vapor and the ice−water interfaces. The ice−aqueous solution interface can be used to generate unique materials. Directional freezing, using a strong thermal gradient, results in kinetic control of ice morphology. Surprisingly, even under these far-from-equilibrium conditions, the secondary prism face is the most stable. A molecularlevel justification of this stability is presented.

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Section: Ice−water Interfacementioning

confidence: 99%

Section: Ice–water Interfacementioning

confidence: 99%

Section: Ice–water Interfacementioning

confidence: 99%

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Ice Interfaces: Vapor, Liquid, and Solutions

Shultz,

Gubbins,

Davies

et al. 2024

J. Phys. Chem. C

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“…Antifreeze proteins (AFPs) and antifreeze glycoproteins (AFGPs) are a kind of special proteins with various antifreeze properties, such as thermal hysteresis (TH), dynamic ice shaping, , and ice recrystallization inhibition, , which can ensure the survival of organisms in the subzero environment , and have attracted extensive research. − Among them, AFGPs are the most effective ice recrystallization inhibitor, which can prevent the melting of small ice crystals and the growth of large ice crystals (i.e., Ostwald ripening) . Due to this unique property, AFGPs have broad application prospects in cryopreservation. , …”

Section: Introductionmentioning

confidence: 99%

Revealing the Mechanism of Irreversible Binding of Antifreeze Glycoproteins to Ice

Zhang

Liu

et al. 2022

J. Phys. Chem. B

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Antifreeze glycoproteins (AFGPs) are a special kind of antifreeze proteins with strong flexibility. Whether their antifreeze activity is achieved by reversibly or irreversibly binding to ice is widely debated, and the molecular mechanism of irreversible binding remains unclear. In this work, the antifreeze mechanism of the smallest AFGP isoform, AFGP8, is investigated at the atomic level.The results indicate that AFGP8 can bind to ice both reversibly through its hydrophobic methyl groups (peptide binding) and irreversibly through its hydrophilic disaccharide moieties (saccharide binding). Although peptide binding occurs faster than saccharide binding, free-energy calculations indicate that the latter is energetically more favorable. In saccharide binding, at least one disaccharide moiety is frozen in the grown ice, resulting in irreversible binding, while the other moieties significantly perturb the water hydrogen-bonding network, thus inhibiting ice growth more effectively. The present study reveals the coexistence of reversible and irreversible bindings of AFGP8, both contributing to the inhibition of ice growth and further provides molecular mechanism of irreversible binding.

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