Observation of ice-like water layers at an aqueous protein surface

Meister, Konrad; Strazdaitė, Simona; DeVries, Arthur L.; Lotze, Stephan; Olijve, Llc Luuk; Voets, Ilja K.; Bakker, Huib J.

doi:10.1073/pnas.1414188111

Cited by 153 publications

(184 citation statements)

References 42 publications

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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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“…The absorbance around 3,200 cm −1 of the IBF surface is stronger, which suggests that there are more ice-like waters on the IBF surface (25). It should be caused by the exposed IBF on the GOPTS surface, on which the regular arrangement of functional groups on IBF organizes bound waters to have an ice-like structure (26).…”

Section: Significancementioning

confidence: 99%

Janus effect of antifreeze proteins on ice nucleation

Liu

Wang

et al. 2016

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

241

187

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The mechanism of ice nucleation at the molecular level remains largely unknown. Nature endows antifreeze proteins (AFPs) with the unique capability of controlling ice formation. However, the effect of AFPs on ice nucleation has been under debate. Here we report the observation of both depression and promotion effects of AFPs on ice nucleation via selectively binding the ice-binding face (IBF) and the non-ice-binding face (NIBF) of AFPs to solid substrates. Freezing temperature and delay time assays show that ice nucleation is depressed with the NIBF exposed to liquid water, whereas ice nucleation is facilitated with the IBF exposed to liquid water. The generality of this Janus effect is verified by investigating three representative AFPs. Molecular dynamics simulation analysis shows that the Janus effect can be established by the distinct structures of the hydration layer around IBF and NIBF. Our work greatly enhances the understanding of the mechanism of AFPs at the molecular level and brings insights to the fundamentals of heterogeneous ice nucleation.antifreeze proteins | ice nucleation | Janus effect | interfacial water | selective tethering A ntifreeze proteins (AFPs) protect a broad range of organisms inhabiting subzero environments. The function of AFPs lies in lowering the freezing point in a noncolligative manner (1, 2). It has been shown that AFPs can adsorb on the ice crystal surface with the ice-binding face (IBF, also termed ice-binding site or icebinding surface) (3, 4). The adsorbed AFPs lead to curvatures on the ice surface between adjacent AFPs, and ice growth is retarded due to the Kelvin effect, which is known as the adsorptioninhibition mechanism (5). However, whether the non-ice-binding face (NIBF) is involved in the function of AFPs and what effect the NIBF exerts are rarely studied (4, 6, 7). On the other hand, the effect of AFPs on ice nucleation (8) is still under intense debate (9-13), although ice nucleation, the formation of a stable nucleus with a critical size, is the control step for ice formation (8). Liu et al. (9) suggested that AFPs could inhibit heterogeneous ice nucleation of water, whereas research on ice nucleation of microdroplets of AFP solutions exhibited no obvious effect of AFPs in inhibiting ice nucleation (10). It was also reported that an AFP solution with high concentration facilitated ice nucleation (11). The contradiction also exists for the research of ice nucleation on solid surfaces immobilized with AFPs (12, 13). Therefore, it is highly desirable to elucidate the exact role of AFPs on ice nucleation and to correlate AFP structures at the molecular level with their function in tuning ice nucleation, which is essential for practical applications in food, pharmaceutical, and chemical industries (14,15).Herein, we investigate the effect of IBF and NIBF of AFPs on ice nucleation via binding AFPs to solid substrates in a way that either IBF or NIBF is exposed to liquid water. This binding method is readily extendable to other AFPs because of the clear distinction...

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“…Possibly, the adsorption of PVA onto ice surfaces is promoted via an indirect interaction of clathrate waters hydrogen-bonded to the hydroxyl groups of the polymer, similar to the binding mechanism of antifreeze proteins to ice surfaces. [30][31][32] Further investigation of the specifi c hydration of PVA may shed light on the adsorption mechanism of PVA onto ice surfaces.…”

Section: Implications For the Ice Binding Of Pvamentioning

confidence: 99%

Influence of Polymer Chain Architecture of Poly(vinyl alcohol) on the Inhibition of Ice Recrystallization

Olijve

Hendrix

Voets

2016

Macromol. Chem. Phys.

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Poly(vinyl alcohol) (PVA) is a water‐soluble synthetic polymer well‐known to effectively block the recrystallization of ice. The effect of polymer chain architecture on the ice recrystallization inhibition (IRI) by PVA remains unexplored. In this work, the synthesis of PVA molecular bottlebrushes is described via a combination of atom‐transfer radical polymerization and reversible addition‐fragmentation chain‐transfer polymerization. The facile preparation of the PVA bottlebrushes is performed via the selective hydrolysis of the chloroacetate esters of the poly(vinyl chloroacetate) (PVClAc) side chains of a PVClAc precursor bottlebrush. The IRI efficacy of the PVA bottlebrush is quantitatively compared to linear PVA. The results show that even if the PVA chains are densely grafted onto a rigid polymer backbone, the IRI activity of PVA is maintained, demonstrating the flexibility in PVA polymer chain architecture for the design of synthetic PVA‐based ice growth inhibitors.

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Observation of ice-like water layers at an aqueous protein surface

Cited by 153 publications

References 42 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

Janus effect of antifreeze proteins on ice nucleation

Influence of Polymer Chain Architecture of Poly(vinyl alcohol) on the Inhibition of Ice Recrystallization

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