Investigates hydration states of glycopolymers affecting lectin binding affinity, indicating implications for biomolecular interactions.
Water is indispensable to life and plays a central role in biological functions. In this study, glycopolymers with distinct backbones (acrylamide or acrylate) and linker lengths (methylene or ethylene) were synthesized via RAFT polymerization to investigate their hydration states. Thermal analysis revealed that glycopolymers with an acrylamide backbone retained more hydration water than those with acrylate backbones. This trend was consistently supported by terahertz spectroscopy and molecular dynamics simulations. In addition, the amount of hydration water increased with increasing linker length. Hemagglutination inhibition assays showed that acrylate-type glycopolymers exhibited markedly higher binding affinity for concanavalin A than their acrylamide-type counterparts across all degrees of polymerization. Importantly, these results reveal a clear inverse correlation between the amount of hydration water and binding affinity, indicating that excessive hydration hinders lectin recognition.
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Kitsuki et al. (2026) studied this question.
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