Antifreeze glycoproteins (AFGPs) are cryoprotective agents that occur naturally in cold-water fish. AFGPs consist of three-residue repeats (Ala-Ala-Thr*)n or (Pro-Ala-Thr*)n, in which a disaccharide is attached to the side-chain of Thr. They adopt a polyproline II helix, with hydrophobic methyl groups (from Ala) on one face and hydrophilic sugars on the opposite face. AFGPs are known to induce thermal hysteresis and to inhibit ice recrystallization. However, the mechanism by which they bind to ice is unclear. Recent molecular dynamics simulations suggest that the methyl groups can “walk” along the ice surface to find properly-spaced cavities, then can reversibly adsorb in order to prevent ice formation. Conversely, another study using fluorescence microscopy indicates that the disaccharides are irreversibly incorporated into the ice crystal lattice. We have attached a water-sensitive naphthalimide fluorophore at various locations throughout an AFGP in order to probe the mode of binding. Unravelling the AFGP-ice interaction would allow for advances in preservation of biological tissues and frozen foods.

Do antifreeze glycopeptides bind to ice reversibly or irreversibly?

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.