Extended Temperature Range of the Ice-Binding Protein Activity

Vera Sirotinskaya, Maya Bar Dolev, Victor Yashunsky, Liat Bahari, Ido Braslavsky*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Ice-binding proteins (IBPs) are expressed in various organisms for several functions, such as protecting them from freezing and freeze injuries. Via adsorption on ice surfaces, IBPs depress ice growth and recrystallization and affect nucleation and ice shaping. IBPs have shown promise in mitigating ice growth under moderate supercooling conditions, but their functionality under cryogenic conditions has been less explored. In this study, we investigate the impact of two types of antifreeze proteins (AFPs): type III AFP from fish and a hyperactive AFP from an insect, the Tenebrio molitor AFP, in vitrified dimethylsulfoxide (DMSO) solutions. We report that these AFPs depress devitrification at −80 °C. Furthermore, in cases where devitrification does occur, AFPs depress ice recrystallization during the warming stage. The data directly demonstrate that AFPs are active at temperatures below the regime of homogeneous nucleation. This research paves the way for exploring AFPs as potential enhancers of cryopreservation techniques, minimizing ice-growth-related damage, and promoting advancements in this vital field.

Original languageAmerican English
Pages (from-to)7395-7404
Number of pages10
JournalLangmuir
Volume40
Issue number14
DOIs
StatePublished - 9 Apr 2024

Bibliographical note

Publisher Copyright:
© 2024 The Authors. Published by American Chemical Society

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