Interaction of ice binding proteins with ice, water and ions

Vrielink, AS Anneloes Oude; Aloi, Antonio; Olijve, Llc Luuk; Voets, Ilja K.

doi:10.1116/1.4939462

Cited by 36 publications

(39 citation statements)

References 167 publications

(224 reference statements)

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“…Unraveling the relative importance of these factors warrants detailed physicochemical experiments (single-molecule imaging, force spectroscopy, sum frequency generation spectroscopy on the ice/water interface, etc.) and accurate (molecular dynamics) simulations (55)(56)(57).…”

Section: Discussionmentioning

confidence: 99%

Blocking rapid ice crystal growth through nonbasal plane adsorption of antifreeze proteins

Olijve

Meister

DeVries

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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147

167

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Antifreeze proteins (AFPs) are a unique class of proteins that bind to growing ice crystal surfaces and arrest further ice growth. AFPs have gained a large interest for their use in antifreeze formulations for water-based materials, such as foods, waterborne paints, and organ transplants. Instead of commonly used colligative antifreezes such as salts and alcohols, the advantage of using AFPs as an additive is that they do not alter the physicochemical properties of the water-based material. Here, we report the first comprehensive evaluation of thermal hysteresis (TH) and ice recrystallization inhibition (IRI) activity of all major classes of AFPs using cryoscopy, sonocrystallization, and recrystallization assays. The results show that TH activities determined by cryoscopy and sonocrystallization differ markedly, and that TH and IRI activities are not correlated. The absence of a distinct correlation in antifreeze activity points to a mechanistic difference in ice growth inhibition by the different classes of AFPs: blocking fast ice growth requires rapid nonbasal plane adsorption, whereas basal plane adsorption is only relevant at long annealing times and at small undercooling. These findings clearly demonstrate that biomimetic analogs of antifreeze (glyco)proteins should be tailored to the specific requirements of the targeted application.antifreeze protein | thermal hysteresis | ice recrystallization inhibition

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Section: Discussionmentioning

confidence: 99%

Blocking rapid ice crystal growth through nonbasal plane adsorption of antifreeze proteins

Olijve

Meister

DeVries

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

147

167

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“…Protein-solvent interactions are especially important in antifreeze proteins (AFP), as they have to specifically recognize and bind -through their Ice Binding Site (IBS) -nucleating ice crystals in the excess of liquid water and prevent further growth of ice 4 . In spite of this seemingly tough goal AFPs show a large structural diversity in nature and are seen in many organisms such as fungi, bacteria, fish, insects, where their major function is to help these organisms survive at subzero temperatures 5 . In addition to their biological role, AFPs also have a variety of applications as ice avoiding agents, from organ preservation 6 to texture enhancers in food 7 .…”

Section: Introductionmentioning

confidence: 99%

Water structure and dynamics in the hydration layer of a type III anti-freeze protein

Brotzakis

Voets

Bakker

et al. 2018

Phys. Chem. Chem. Phys.

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We report on a molecular dynamics study on the relation between the structure and the orientational (and hydrogen bond) dynamics of hydration water around the ocean pout AFP III anti-freeze protein. We find evidence for an increasing tetrahedral structure from the area opposite to the ice binding site (IBS) towards the protein IBS, with the strongest signal of tetrahedral structure around the THR-18 residue of the IBS. The tetrahedral structural parameter mostly positively correlates with increased reorientation decay times. Interestingly, for several key (polar) residues that are not part of the IBS but are in its vicinity, we observe a decrease of the reorientation time with increasing tetrahedral structure. A similar anti-correlation is observed for the hydrogen-bonded water molecules. These effects are enhanced at a lower temperature. We interpret these results in terms of the structure-making and structure-breaking residues. Moreover, we investigate the tetrahedral structure and dynamics of waters at a partially dehydrated IBS, and for the protein adsorbed at the air-water interface. We find that the mutation changes the preferred protein orientation upon adsorption at an air-water interface. These results are in agreement with the water-air Vibration Sum Frequency Generation spectroscopic experiments showing a strongly reduced tetrahedral signal upon mutation at the IBS.

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“…While there are much smaller frozen canals on c photo, there is small ice crystals in the d picture, even in the unfrozen canals (black arrow) [87]. intracellular ice formation and recrystallization has been demonstrated in yeast, plant cells [91], hamster tissue culture cells [92], and turkey sperm [93]. During defrosting, recrystallization generally starts at −40°C, and it becomes intense at the temperature range of −25 to −20°C.…”

Section: Damage During Thawingmentioning

confidence: 98%

Cryobiology and Cryopreservation of Sperm

Öztürk¹,

Bucak²,

Bodu³

et al. 2020

Cryopreservation - Current Advances and Evaluations

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Low temperature has been utilized to keep living cells and tissues dormant but potentially alive for cryopreservation and biobanking with great impacts on scientific and biomedical applications. However, there is a critical contradiction between the purpose of the cryopreservation and experimental findings: the cryopreserved cells and tissues can be fatally damaged by the cryopreservation process itself. Contrary to popular belief, the challenge to the life of living cells and tissues during the cryopreservation is not their ability to endure storage at cryogenic temperatures (below −190°C); rather it is the lethality associated with mass and energy transport within an intermediate zone of low temperature (−15 to −130°C) that a cell must traverse twice, once during cooling and once during warming. This chapter will focus on (1) the mechanisms of cryoinjury and cryopretection of human sperm in cryopreservation, and (2) cryopreservation techniques and methods developed based on the understanding of the above mechanisms.2 can be caused to the cells during the cryopreservation process. In this review, the mechanisms of damage to the sperm cells during the process of cryopreservation will be taken under spotlight and we will try to elucidate them in a causeeffect manner. What is cryobiology?Cryobiology is a multidisciplinary science, studying the physical and biological behaviors of living materials (e.g., cells and tissues) at low temperatures. Cryobiology contains many disciplines such as, cellular biology, theriogenology and molecular biology, engineering and mathematics, veterinary and human medicine, intensive and extensive farming on land and in watery environments [6]. Optimization of the cryopreservation procedure of spermatozoa needs all the above-mentioned disciplines because of the complex cellular structure, activation and capacitation mechanisms of spermatozoon [7].

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Interaction of ice binding proteins with ice, water and ions

Cited by 36 publications

References 167 publications

Blocking rapid ice crystal growth through nonbasal plane adsorption of antifreeze proteins

Blocking rapid ice crystal growth through nonbasal plane adsorption of antifreeze proteins

Water structure and dynamics in the hydration layer of a type III anti-freeze protein

Cryobiology and Cryopreservation of Sperm

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