The antifreeze mechanism of antifreeze
proteins (AFPs) evolved
by organisms has been widely studied. However, detailed knowledge
of the synergy between AFPs and ice crystals still remains fragmentary.
In the present contribution, the cooperative effect of the hyperactive
insect antifreeze protein TmAFP and ice crystals
on the interfacial water during the entire process of inhibiting ice
growth is systematically investigated at the atomic level and compared
with its low activity mutant and a nonantifreeze protein. The results
indicate a significant synergy between TmAFP and
ice crystals, which enables the TmAFP to promote
the ice growth before adsorbing on the surfaces of the ice crystals,
while the mutant and the nonantifreeze protein cannot promote the
ice growth due to the lack of this synergy. When TmAFP approaches the ice surface, the interfacial water is induced
by both the AFP and the ice crystals to form the anchored clathrate
motif, which binds TmAFP to the ice surface, resulting
in a local increase in the curvature of the ice surface, thereby inhibiting
the growth of ice. In this study, three stages, namely, promotion,
adsorption, and inhibition, are observed in the complete process of TmAFP inhibiting ice growth, and the synergistic mechanism
between protein and ice crystals is revealed. The results are helpful
for the design of antifreeze proteins and bioinspired antifreeze materials
with superior performance.
The binding of antifreeze proteins (AFPs) to ice needs to be mediated by interfacial water molecules. Our previous study of the effect of AFPs on the dynamics of the interfacial...
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