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      From ice-binding proteins to bio-inspired antifreeze materials

      review-article
      a , b , c
      Soft Matter
      Royal Society of Chemistry

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          Abstract

          Ice-binding proteins (IBP) facilitate survival under extreme conditions in diverse life forms. Successful translation of this natural cryoprotective ability into man-made materials would open up new avenues in biomedicine, agrifood and materials science. This review covers recent advances in the field of IBPs and their synthetic analogues, focusing on fundamental insights of biological and technological relevance.

          Abstract

          Ice-binding proteins (IBP) facilitate survival under extreme conditions in diverse life forms. IBPs in polar fishes block further growth of internalized environmental ice and inhibit ice recrystallization of accumulated internal crystals. Algae use IBPs to structure ice, while ice adhesion is critical for the Antarctic bacterium Marinomonas primoryensis. Successful translation of this natural cryoprotective ability into man-made materials holds great promise but is still in its infancy. This review covers recent advances in the field of ice-binding proteins and their synthetic analogues, highlighting fundamental insights into IBP functioning as a foundation for the knowledge-based development of cheap, bio-inspired mimics through scalable production routes. Recent advances in the utilisation of IBPs and their analogues to e.g. improve cryopreservation, ice-templating strategies, gas hydrate inhibition and other technologies are presented.

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          Adsorption inhibition as a mechanism of freezing resistance in polar fishes.

          Polar fishes are known to have serum proteins and glycoproteins that protect them from freezing, by a noncolligative process. Measurements of antifreeze concentrations in ice and scanning electron micrographs of freeze-dried antifreeze solutions indicate that the antifreezes are incorporated in ice during freezing. The antifreezes also have a pronounced effect on the crystal habit of ice grown in their presence. Each of four antifreezes investigated caused ice to grow in long needles whose axes were parallel to the ice c axis. Together these results indicate the antifreezes adsorb to ice surfaces and inhibit their growth. A model in which adsorbed antifreezes raise the curvature of growth steps on the ice surface is proposed to account for the observed depression of the temperature at which freezing occurs and agrees well with experimental observations. The model is similar to one previously proposed for other cases of crystal growth inhibition.
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            Ice-binding proteins: a remarkable diversity of structures for stopping and starting ice growth.

            Antifreeze proteins (AFPs) were discovered in marine fishes that need protection from freezing. These ice-binding proteins (IBPs) are widespread across biological kingdoms, and their functions include freeze tolerance and ice adhesion. Consistent with recent independent evolution, AFPs have remarkably diverse folds that rely heavily on hydrogen- and disulfide-bonding. AFP ice-binding sites are typically flat, extensive, relatively hydrophobic, and are thought to organize water into an ice-like arrangement that merges and freezes with the quasi-liquid layer next to the ice lattice. In this article, the roles, properties, and structure-function interactions of IBPs are reviewed, and their relationship to ice nucleation proteins, which promote freezing at high subzero temperatures, is explored.
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              Antifreeze proteins in overwintering plants: a tale of two activities.

              Antifreeze proteins are found in a wide range of overwintering plants where they inhibit the growth and recrystallization of ice that forms in intercellular spaces. Unlike antifreeze proteins found in fish and insects, plant antifreeze proteins have multiple, hydrophilic ice-binding domains. Surprisingly, antifreeze proteins from plants are homologous to pathogenesis-related proteins and also provide protection against psychrophilic pathogens. In winter rye (Secale cereale), antifreeze proteins accumulate in response to cold, short daylength, dehydration and ethylene, but not pathogens. Transferring single genes encoding antifreeze proteins to freezing-sensitive plants lowered their freezing temperatures by approximately 1 degrees C. Genes encoding dual-function plant antifreeze proteins are excellent models for use in evolutionary studies to determine how genes acquire new expression patterns and how proteins acquire new activities.
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                Author and article information

                Journal
                Soft Matter
                Soft Matter
                Soft Matter
                Royal Society of Chemistry
                1744-683X
                1744-6848
                28 July 2017
                16 June 2017
                : 13
                : 28
                : 4808-4823
                Affiliations
                [a ] Institute for Complex Molecular Systems , Eindhoven University of Technology , Post Office Box 513 , 5600 MD Eindhoven , The Netherlands . Email: I.Voets@ 123456tue.nl
                [b ] Laboratory of Macromolecular and Organic Chemistry , Department of Chemical Engineering and Chemistry , Eindhoven University of Technology , Post Office Box 513 , 5600 MD Eindhoven , The Netherlands
                [c ] Laboratory of Physical Chemistry , Department of Chemical Engineering and Chemistry , Eindhoven University of Technology , Post Office Box 513 , 5600 MD Eindhoven , The Netherlands
                Author information
                http://orcid.org/0000-0003-3543-4821
                Article
                c6sm02867e
                10.1039/c6sm02867e
                5708349
                28657626
                239101c3-44a8-41d0-ac8d-1c5ce81468da
                This journal is © The Royal Society of Chemistry 2017

                This article is freely available. This article is licensed under a Creative Commons Attribution Non Commercial 3.0 Unported Licence (CC BY-NC 3.0)

                History
                : 23 December 2016
                : 16 June 2017
                Categories
                Chemistry

                Soft matter
                Soft matter

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