AI Article Synopsis
- Antifreeze proteins (AFPs) prevent ice crystal growth by interacting specifically with ice surfaces, with hyperactive AFPs having a unique threonine-rich motif for binding.
- Research revealed that the hydration layer around the non-ice-binding surface (non-IBS) of hyperactive AFPs is liquid-like, contrasting with the ice-like hydration around the ice-binding surface (IBS), even in cold conditions.
- The study highlights differences in amino acid composition and arrangement between the IBS, non-IBS, and non-AFP surfaces, demonstrating how both surfaces work together to inhibit ice growth: the IBS for binding to ice and the non-IBS for preventing ice formation.
Article Abstract
Antifreeze proteins (AFPs) show thermal hysteresis through specific interaction with the ice crystal. Hyperactive AFPs interact with the ice surface through a threonine-rich motif present at their ice-binding surface (IBS). Ordering of water around the IBS was extensively investigated. However, the role of non-IBS in ice growth inhibition is yet to be understood completely. The present study explores the nature of hydration and its length-scale evaluation around the non-IBS for hyperactive AFPs. We observed that the hydration layer of non-IBS is liquid-like, even in highly supercooled conditions, and the nature of hydration is drastically different from the hydration pattern of non-AFP surfaces. In similar conditions, the hydration layer around the IBS is ice-like ordered. Non-IBS of the hyperactive AFP exposes toward the bulk and is able to maintain the liquid-like character of its hydration water up to 15 Å. We also find that the amino acid compositions and their spatial distribution on the non-IBS are markedly different from those of the IBS and non-AFP surfaces. These results elucidate the combined role of IBS and non-IBS in ice-growth inhibition. While IBS is required to adsorb on ice efficiently, the exposed non-IBS may prevent ice nucleation/growth on top of the bound AFPs.
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| http://dx.doi.org/10.1021/acs.jpcb.0c01206 | DOI Listing |
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