Proline-Mediated Conformational Rigidity Governs the Ice-Binding Behavior of Antifreeze Glycopeptides

Jingwen Zhang; Haipeng Wang; Xuyang Liu; Xueguang Shao; Wensheng Cai

doi:10.1039/d5cp05048k

January 1, 2026Physical Chemistry Chemical Physics

Proline-Mediated Conformational Rigidity Governs the Ice-Binding Behavior of Antifreeze Glycopeptides

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Key Points

This research aims to understand how proline mutations influence the ice-binding activity of antifreeze glycopeptides.
Analyzed the structural effects of proline mutations in short antifreeze glycopeptides.
Investigated the relationship between conformational rigidity and ice recrystallization inhibition.
Proline mutations significantly alter the conformational rigidity of antifreeze glycopeptides.
Increased rigidity correlates with enhanced inhibition of ice recrystallization.

Implication

Investigates how proline mutations affect ice recrystallization in antifreeze glycoproteins, suggesting mechanisms of action.

Abstract

Antifreeze glycoproteins (AFGPs) are among the most potent inhibitors of ice recrystallization, yet the conformational basis of their activity and the effects of Proline mutations in short AFGP peptides remain...

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Cite This Study

Zhang et al. (2026) studied this question.

synapsesocial.com/papers/69be361e6e48c4981c674cfa https://doi.org/10.1039/d5cp05048k

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Proline-Mediated Conformational Rigidity Governs the Ice-Binding Behavior of Antifreeze Glycopeptides

Key Points

Implication

Abstract

Discussion

Cite This Study

Proline-Mediated Conformational Rigidity Governs the Ice-Binding Behavior of Antifreeze Glycopeptides

Key Points

Implication

Abstract

Discussion

Cite This Study

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