Investigation of ice binding proteins applications for cryopreservation of biological systems

Sirotinskaya, Vera; Bein, Amir; Braslavsky, Ido

doi:10.1016/j.cryobiol.2016.09.151

Cited by 1 publication

(4 citation statements)

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“…Ice recrystallization inhibition of vitrified AFP in 40% DMSO solutions at −50 °C. Scale bar = 50 μM …”

Section: Resultsmentioning

confidence: 99%

“…(*) p < 0.01, compared to the value of no protein and BSA at equimolar concentrations. 49 BSA led to 75% "+Devit" and 25% "∓Devit". Both the "+Devit" and "∓Devit" morphologies are predominantly aligned with the category of "metastable vitrification", suggesting that the effect of BSA is not necessarily significant.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

“…(D) "++Devit" which indicates the rapid growth of densely populated ice nuclei to form a bulk of ice (images taken at 40% DMSO). Scale bar = 200 μm 49.…”

mentioning

confidence: 99%

“…The data represent the mean value ± standard error of the mean (SEM), N ≥ 14 in all experiments.The data were analyzed with a one-way analysis of variance (ANOVA), followed by a comparison of experimental groups with the appropriate control group (Tukey's post hoc test). (*) p < 0.01, compared to the value of no protein and BSA at equimolar concentrations 49.…”

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confidence: 99%

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Extended Temperature Range of the Ice-Binding Protein Activity

Sirotinskaya,

Bar Dolev,

Yashunsky

et al. 2024

Langmuir

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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 icegrowth-related damage, and promoting advancements in this vital field.

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“…Ice recrystallization inhibition of vitrified AFP in 40% DMSO solutions at −50 °C. Scale bar = 50 μM …”

Section: Resultsmentioning

confidence: 99%

Section: ■ Materials and Methodsmentioning

confidence: 99%

“…(D) "++Devit" which indicates the rapid growth of densely populated ice nuclei to form a bulk of ice (images taken at 40% DMSO). Scale bar = 200 μm 49.…”

mentioning

confidence: 99%

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confidence: 99%

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