ArticleThe journal of physical chemistry. B2014
Perturbation of long-range water dynamics as the mechanism for the antifreeze activity of antifreeze glycoprotein.
Article in The journal of physical chemistry. B, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 38 citations in OpenAlex.
- Adsorption Barrier Limits the Ice Inhibition Activity of Glycan-Rich Antifreeze Glycoproteins.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Biomimetic Localized Gel Electrolyte for Practical Zinc Anode.Angewandte Chemie (International ed. in English) · 2025Article
- Cooperative Role of Conformation and Ice-Binding Groups in Ice Growth Inhibition of Antifreeze Glycoproteins.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Review
- Protein 3D Hydration: A Case of Bovine Pancreatic Trypsin Inhibitor.International journal of molecular sciences · 2022Article
- The Ensemble of Conformations of Antifreeze Glycoproteins (AFGP8): A Study Using Nuclear Magnetic Resonance Spectroscopy.Biomolecules · 2019Article
- Synthesis and conformational preferences of short analogues of antifreeze glycopeptides (AFGP).Beilstein journal of organic chemistry · 2019Article
- Balance between hydration enthalpy and entropy is important for ice binding surfaces in Antifreeze Proteins.Scientific reports · 2017Article
- Antifreeze glycopeptides: from structure and activity studies to current approaches in chemical synthesis.Amino acids · 2017Review
- Structure-activity relationship of the exopolysaccharide from a psychrophilic bacterium: A strategy for cryoprotection.Carbohydrate polymers · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Very little is known about the mechanism of antifreeze action of antifreeze glycoproteins (AFGPs) present in Antarctic teleost fish. Recent NMR and CD studies assisted with total synthesis of synthetic AFGP variants have provided insight into the structure of short AFGP glycopeptides, though the observations did not yield information on the antifreeze mechanism of action. In this study, we use Hamiltonian replica exchange (HREX) molecular dynamics simulations to probe the structure and surrounding aqueous environments of both the natural (AFGP8) and synthetic (s-AFGP4) AFGPs. AFGPs can adopt both amphiphilic and pseudoamphiphilic conformations, the preference of which is related to the proline content of the peptide. The arrangement of carbohydrates allows the hydroxyl groups on terminal galactose units to form stable water bridges which in turn influence the hydrogen-bond network, structure, and dynamics of the surrounding solvent. Interestingly, these local effects lead to the perturbation of the tetrahedral environment for water molecules in hydration layers far (10.0-12.0 Å) from the AFGPs. This structure-induced alteration of long-range hydration dynamics is proposed to be the major contributor to antifreeze activity, a conclusion that is in line with terahertz spectroscopy experiments. The detailed structure-mechanism correlation provided in this study could lead to the design of better synthetic AFGP variants.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.