An Ultrapotent, Ultraeconomical, Antifreeze Polypeptide

The growth of large ice crystals during freeze and thaw events is a challenge in diverse settings from transportation and agriculture to foods and biomedicine. Design, synthesis, and evaluation of antifreeze polypeptides that inhibit ice crystal growth at µg concentrations are reported herein. The polypeptides, composed of Ala and Glu, are prepared using economical methodology, are stable after thermal events, are biodegradable, and are nontoxic to human cells. Mirror-image polypeptides have resisted degradation and are suitable for applications with a longevity criterion. Their α-helical conformation plays a role in antifreeze activity, but chirality does not. In proof-of-concept experiments, the antifreeze polypeptides could prevent damage to model protein therapeutics during repeated freeze-thaw cycles and could be applied to prevent large ice crystals in a frozen food product. These simple, economical Ala/Glu polypeptides are promising materials for diverse antifreeze applications, particularly in biological settings.

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Publication Details

Journal
Advanced Materials
Published
2025-08-28
DOI
https://doi.org/10.1002/adma.202420504
Citations
3
Primary Topic
Physiological and biochemical adaptations
Type
article
Field-Weighted Citation Impact
5.15

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article

An Ultrapotent, Ultraeconomical, Antifreeze Polypeptide

Rachel E. Detwiler, Konrad Meister, Ke Wang, Charles T. Osborne et al.
3 citations
Advanced Materials
Physiological and biochemical adaptations
5.15
article

An Ultrapotent, Ultraeconomical, Antifreeze Polypeptide

Rachel E. Detwiler, Konrad Meister, Ke Wang, Charles T. Osborne, Jessica R. Kramer, Thomas J. McPartlon
article en
3 citations

Abstract

The growth of large ice crystals during freeze and thaw events is a challenge in diverse settings from transportation and agriculture to foods and biomedicine. Design, synthesis, and evaluation of antifreeze polypeptides that inhibit ice crystal growth at µg concentrations are reported herein. The polypeptides, composed of Ala and Glu, are prepared using economical methodology, are stable after thermal events, are biodegradable, and are nontoxic to human cells. Mirror-image polypeptides have resisted degradation and are suitable for applications with a longevity criterion. Their α-helical conformation plays a role in antifreeze activity, but chirality does not. In proof-of-concept experiments, the antifreeze polypeptides could prevent damage to model protein therapeutics during repeated freeze-thaw cycles and could be applied to prevent large ice crystals in a frozen food product. These simple, economical Ala/Glu polypeptides are promising materials for diverse antifreeze applications, particularly in biological settings.

Advanced MaterialsVol. 38(4)
Boise State University (US), University of Utah (US)
National Science Foundation, Division of Materials Research
Openalex Percentile: Top 5%
Physiological and biochemical adaptations
5.15
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