Molecular Recognition of Ice by Fully Flexible Molecules

PM Naullage and L Lupi and V Molinero, JOURNAL OF PHYSICAL CHEMISTRY C, 121, 26949-26957 (2017).

DOI: 10.1021/acs.jpcc.7b10265

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 matching between the hydroxyl groups of PVA and water molecules at the ice surface. Strong, cooperative binding to ice results from the different scaling of the free energy gains on binding per monomer and the loss of translational and configurational entropy of the chain. We explain why branching of PVA does not improve its IRI activity and use the new molecular understanding to propose principles for the design of macromolecules that bind efficiently to the basal and prismatic planes of ice, producing hyperactive synthetic antifreeze molecules that could compete with the most effective antifreeze proteins.

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