ArticlePhilosophical transactions. Series A, Mathematical, physical, and engineering sciences2019
Ice-binding proteins and the applicability and limitations of the kinetic pinning model.
Article in Philosophical transactions. Series A, Mathematical, physical, and engineering sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- Adsorption Barrier Limits the Ice Inhibition Activity of Glycan-Rich Antifreeze Glycoproteins.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Atomistic Insights into the Chain-Length-Dependent Antifreeze Activity of Oligoprolines.Biomacromolecules · 2025Article
- Extended Temperature Range of the Ice-Binding Protein Activity.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- Psychrophiles to control ice-water phase changes in frost-susceptible soils.Scientific reports · 2024Article
- Nanoscopy of single antifreeze proteins reveals that reversible ice binding is sufficient for ice recrystallization inhibition but not thermal hysteresis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Regulated strategies of cold-adapted microorganisms in response to cold: a review.Environmental science and pollution research international · 2021Review
- The physics and chemistry of ice.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Ice-binding proteins (IBPs) are unique molecules that bind to and are active on the interface between two phases of water: ice and liquid water. This property allows them to affect ice growth in multiple ways: shaping ice crystals, suppressing the freezing point, inhibiting recrystallization and promoting nucleation. Advances in the protein's production technologies make these proteins promising agents for medical applications among others. Here, we focus on a special class of IBPs that suppress freezing by causing thermal hysteresis (TH): antifreeze proteins (AFPs). The kinetic pinning model describes the dynamics of a growing ice face with proteins binding to it, which eventually slow it down to a halt. We use the kinetic pinning model, with some adjustments made, to study the TH dependence on the solution's concentration of AFPs by fitting the model to published experimental data. We find this model describes the activity of (moderate) type III AFPs well, but is inadequate for the (hyperactive) Tenebrio molitor AFPs. We also find the engulfment resistance to be a key parameter, which depends on the protein's size. Finally, we explain intuitively how TH depends on the seeding time of the ice crystal in the protein solution. Using this insight, we explain the discrepancy in TH measurements between different assays. This article is part of the theme issue 'The physics and chemistry of ice: scaffolding across scales, from the viability of life to the formation of planets'.
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