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Ice-binding proteins and bioinspired synthetic mimics in non-physiological environments

Ice-binding proteins (IBPs) are produced by a variety of organisms to prevent internal damage caused by ice crystal growth. Synthetic analogs are being designed to mimic beneficial properties of IBPs while mitigating drawbacks related to the use of biological proteins. While a multitude of engineeri...

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Detalles Bibliográficos
Autores principales: Delesky, Elizabeth A., Srubar, Wil V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9097698/
https://www.ncbi.nlm.nih.gov/pubmed/35573196
http://dx.doi.org/10.1016/j.isci.2022.104286
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author Delesky, Elizabeth A.
Srubar, Wil V.
author_facet Delesky, Elizabeth A.
Srubar, Wil V.
author_sort Delesky, Elizabeth A.
collection PubMed
description Ice-binding proteins (IBPs) are produced by a variety of organisms to prevent internal damage caused by ice crystal growth. Synthetic analogs are being designed to mimic beneficial properties of IBPs while mitigating drawbacks related to the use of biological proteins. While a multitude of engineering applications could benefit from the inhibition and control of ice formation and growth, synthetic analogs tend to be less potent than biological IBPs, and both IBPs and synthetic analogs tend to exhibit lower performance in non-physiological (i.e., non-biological) solutions. This review examines the ice interaction properties and performance of IBPs and their synthetic analogs in non-physiological environments. Common methods to measure ice interactions are discussed (i.e., thermal hysteresis, ice recrystallization inhibition, ice growth rate, and ice nucleation). A quantitative meta-analysis of material performance in non-physiological environments is presented, along with a discussion of future research directions. The findings presented herein can inform IBP and synthetic mimic selection to control ice interactions in a wide variety of materials science and engineering applications, including cell, tissue, and organ cryopreservation, food storage and transport, freeze-thaw damage of cementitious materials, and anti-icing surfaces for aerospace vehicles, solar panels, and wind turbines.
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spelling pubmed-90976982022-05-13 Ice-binding proteins and bioinspired synthetic mimics in non-physiological environments Delesky, Elizabeth A. Srubar, Wil V. iScience Review Ice-binding proteins (IBPs) are produced by a variety of organisms to prevent internal damage caused by ice crystal growth. Synthetic analogs are being designed to mimic beneficial properties of IBPs while mitigating drawbacks related to the use of biological proteins. While a multitude of engineering applications could benefit from the inhibition and control of ice formation and growth, synthetic analogs tend to be less potent than biological IBPs, and both IBPs and synthetic analogs tend to exhibit lower performance in non-physiological (i.e., non-biological) solutions. This review examines the ice interaction properties and performance of IBPs and their synthetic analogs in non-physiological environments. Common methods to measure ice interactions are discussed (i.e., thermal hysteresis, ice recrystallization inhibition, ice growth rate, and ice nucleation). A quantitative meta-analysis of material performance in non-physiological environments is presented, along with a discussion of future research directions. The findings presented herein can inform IBP and synthetic mimic selection to control ice interactions in a wide variety of materials science and engineering applications, including cell, tissue, and organ cryopreservation, food storage and transport, freeze-thaw damage of cementitious materials, and anti-icing surfaces for aerospace vehicles, solar panels, and wind turbines. Elsevier 2022-04-22 /pmc/articles/PMC9097698/ /pubmed/35573196 http://dx.doi.org/10.1016/j.isci.2022.104286 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Review
Delesky, Elizabeth A.
Srubar, Wil V.
Ice-binding proteins and bioinspired synthetic mimics in non-physiological environments
title Ice-binding proteins and bioinspired synthetic mimics in non-physiological environments
title_full Ice-binding proteins and bioinspired synthetic mimics in non-physiological environments
title_fullStr Ice-binding proteins and bioinspired synthetic mimics in non-physiological environments
title_full_unstemmed Ice-binding proteins and bioinspired synthetic mimics in non-physiological environments
title_short Ice-binding proteins and bioinspired synthetic mimics in non-physiological environments
title_sort ice-binding proteins and bioinspired synthetic mimics in non-physiological environments
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9097698/
https://www.ncbi.nlm.nih.gov/pubmed/35573196
http://dx.doi.org/10.1016/j.isci.2022.104286
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