Abstract
Antifreeze proteins are produced by extremophile species to control ice formation and growth, and they have potential applications in many fields. There are few examples of synthetic materials which can reproduce their potent ice recrystallization inhibition property. We report that self-assembled enantiomerically pure, amphipathic metallohelicies inhibited ice growth at just 20 μM. Structure–property relationships and calculations support the hypothesis that amphipathicity is the key motif for activity. This opens up a new field of metallo-organic antifreeze protein mimetics and provides insight into the origins of ice-growth inhibition.
Highlights
Antifreezeproteins [AF(G)Ps] from the blood of polar fish enable life to flourish in hostile, ice-rich environments.[1]
AF(G)Ps have several unique macroscopic properties including ice shaping and the non-colligative depression of the freezing point. Their property of ice recrystallization inhibition (IRI) slowing of ice growth is of great technological interest
Ben and co-workers reported that short glycopeptides with a simplified amino acid sequence were potent IRIs but did not display any ice shaping or freezing point depression.[10−12] This implied that a specific receptor−ligand type of interaction is not essential for IRI and that more diverse structures could potentially have useful activity, but most reports still required complex synthesis.[12]
Summary
Antifreeze (glyco)proteins [AF(G)Ps] from the blood of polar fish enable life to flourish in hostile, ice-rich environments.[1]. We report here the unprecedented IRI activity of these compounds, and we suggest, based on hydrophobicity calculations and structural analyses, that the activity stems from amphipathic charge distribution.
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