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Janus effect of antifreeze proteins on ice nucleation.


ABSTRACT: 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.

SUBMITTER: Liu K 

PROVIDER: S-EPMC5187720 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

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Janus effect of antifreeze proteins on ice nucleation.

Liu Kai K   Wang Chunlei C   Ma Ji J   Shi Guosheng G   Yao Xi X   Fang Haiping H   Song Yanlin Y   Wang Jianjun J  

Proceedings of the National Academy of Sciences of the United States of America 20161207 51


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 ass  ...[more]

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