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From ice-binding proteins to bio-inspired antifreeze materials

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 critic...

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Detalles Bibliográficos
Autor principal: Voets, I. K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5708349/
https://www.ncbi.nlm.nih.gov/pubmed/28657626
http://dx.doi.org/10.1039/c6sm02867e
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author Voets, I. K.
author_facet Voets, I. K.
author_sort Voets, I. K.
collection PubMed
description 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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spelling pubmed-57083492018-01-05 From ice-binding proteins to bio-inspired antifreeze materials Voets, I. K. Soft Matter Chemistry 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. Royal Society of Chemistry 2017-07-28 2017-06-16 /pmc/articles/PMC5708349/ /pubmed/28657626 http://dx.doi.org/10.1039/c6sm02867e Text en This journal is © The Royal Society of Chemistry 2017 http://creativecommons.org/licenses/by-nc/3.0/ 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)
spellingShingle Chemistry
Voets, I. K.
From ice-binding proteins to bio-inspired antifreeze materials
title From ice-binding proteins to bio-inspired antifreeze materials
title_full From ice-binding proteins to bio-inspired antifreeze materials
title_fullStr From ice-binding proteins to bio-inspired antifreeze materials
title_full_unstemmed From ice-binding proteins to bio-inspired antifreeze materials
title_short From ice-binding proteins to bio-inspired antifreeze materials
title_sort from ice-binding proteins to bio-inspired antifreeze materials
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5708349/
https://www.ncbi.nlm.nih.gov/pubmed/28657626
http://dx.doi.org/10.1039/c6sm02867e
work_keys_str_mv AT voetsik fromicebindingproteinstobioinspiredantifreezematerials