Abstract
Cold acclimatized organisms produce antifreeze proteins that prevent ice growth and recrystallization at subfreezing conditions. Flatness and rigidity of the ice-binding sites of antifreeze proteins are considered key for their recognition of ice. However, the most potent synthetic ice recrystallization inhibitor (IRI) found to date is poly(vinyl alcohol) (PVA), a fully flexible molecule. The ability to tune the architecture and functionalization of PVA makes it a promising candidate to replace antifreeze proteins in industrial applications ranging from cryopreservation of organs to deicing of turbine blades. However, an understanding of how does PVA recognize ice remains elusive, hampering the design of more effective IRIs. Here we use large-scale molecular simulations to elucidate the mechanism by which PVA recognizes ice. We find that the polymer selectively binds to the prismatic faces of ice through a cooperative zipper mechanism. The binding is driven by hydrogen bonding, facilitated by distance mat...
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