ArticleInternational journal of biological macromolecules2019
A beetle antifreeze protein protects lactate dehydrogenase under freeze-thawing.
Article in International journal of biological macromolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Ice-binding protein's dual roles for prolonging the enzymatic activity of alcohol dehydrogenase against freezing.International journal of biological macromolecules · 2026Article
- Natural compounds as lactate dehydrogenase inhibitors: potential therapeutics for lactate dehydrogenase inhibitors-related diseases.Frontiers in pharmacology · 2023Review
- Submilligram Level of Beetle Antifreeze Proteins Minimize Cold-Induced Cell Swelling and Promote Cell Survival.Biomolecules · 2022Article
- Toxicity profiles and protective effects of antifreeze proteins from insect in mammalian models.Toxicology letters · 2022Article
- Protection of Alcohol Dehydrogenase against Freeze-Thaw Stress by Ice-Binding Proteins Is Proportional to Their Ice Recrystallization Inhibition Property.Marine drugs · 2020Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Effects of a beetle antifreeze proteins (AFP) from Dendroides canadensis (DAFP-1) on a model freeze-labile enzyme, lactate dehydrogenase (LDH), were investigated under freezing and thawing conditions. The presence of DAFP-1 can effectively protect the enzymatic activity of LDH upon repeated freezing and thawing and the protective role of DAFP-1 is more significant than that of bovine serum albumin (BSA), a common protectant for freeze-labile proteins. The results of circular dichroism (CD) spectroscopy suggest that the presence of DAFP-1 provides protection to the denaturation of LDH under freezing and thawing. The molecular dynamics (MD) simulation of DAFP-1 and LDH suggests that DAFP-1 interacts with LDH using its ice-binding surface (IBS) and mainly through its arginine residues. A mutant of DAFP-1, where all the arginine residues were replaced by alanine residues, lost its effect in protecting LDH under freezing and thawing. The results demonstrated that DAFP-1 is an effective protectant for a freeze-labile protein under freezing and thawing and the arginine residues in DAFP-1 are important for its protective role. By correlating the protective effect of an AFP with its structure, new insights in the identification and development of effective protectants for freeze-labile proteins were provided.
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Registered trials
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