ArticleBiomolecules2020
Fish-Derived Antifreeze Proteins and Antifreeze Glycoprotein Exhibit a Different Ice-Binding Property with Increasing Concentration.
Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Article
- An Ultrapotent, Ultraeconomical, Antifreeze Polypeptide.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- How to measure the activity of antifreeze proteins?Biophysical reviews · 2025Review
- Effect of Antifreeze Glycopeptides on the Quality and Microstructure of Frozen Lamb Meatballs.Metabolites · 2025Article
- Synthetic Antifreeze Glycoproteins with Potent Ice-Binding Activity.Chemistry of materials : a publication of the American Chemical Society · 2024Article
- Subzero Nonfreezing Hypothermia with Insect Antifreeze Protein Dramatically Improves Survival Rate of Mammalian Cells.International journal of molecular sciences · 2021Article
- Laboratory diffracted x-ray blinking to monitor picometer motions of protein molecules and application to crystalline materials.Structural dynamics (Melville, N.Y.) · 2021Article
- Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity.Scientific reports · 2021Article
- An Ice-Binding Protein from an Antarctic Ascomycete Is Fine-Tuned to Bind to Specific Water Molecules Located in the Ice Prism Planes.Biomolecules · 2020Article
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Authors and funding
7 authors.
Funding
Abstract
The concentration of a protein is highly related to its biochemical properties, and is a key determinant for its biotechnological applications. Antifreeze proteins (AFPs) and antifreeze glycoproteins (AFGPs) are structurally diverse macromolecules that are capable of binding to embryonic ice crystals below 0 °C, making them useful as protectants of ice-block formation. In this study, we examined the maximal solubility of native AFP I-III and AFGP with distilled water, and evaluated concentration dependence of their ice-binding property. Approximately 400 mg/mL (AFP I), 200 mg/mL (AFP II), 100 mg/mL (AFP III), and >1800 mg/mL (AFGP) of the maximal solubility were estimated, and among them AFGP's solubility is much higher compared with that of ordinary proteins, such as serum albumin (~500 mg/mL). The samples also exhibited unexpectedly high thermal hysteresis values (2-3 °C) at 50-200 mg/mL. Furthermore, the analysis of fluorescence-based ice plane affinity showed that AFP II binds to multiple ice planes in a concentration-dependent manner, for which an oligomerization mechanism was hypothesized. The difference of concentration dependence between AFPs and AFGPs may provide a new clue to help us understand the ice-binding function of these proteins.
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