Hydration Shell of Antifreeze Proteins: Unveiling the Role of Non-Ice-Binding Surfaces

2019 ◽  
Vol 123 (30) ◽  
pp. 6474-6480 ◽  
Author(s):  
Laura Zanetti-Polzi ◽  
Akash Deep Biswas ◽  
Sara Del Galdo ◽  
Vincenzo Barone ◽  
Isabella Daidone
Keyword(s):  
Antifreeze Proteins ◽  
Hydration Shell ◽  
Ice Binding

scholarly journals Janus effect of antifreeze proteins on ice nucleation

2016 ◽  
Vol 113 (51) ◽  
pp. 14739-14744 ◽  
Author(s):  
Kai Liu ◽  
Chunlei Wang ◽  
Ji Ma ◽  
Guosheng Shi ◽  
Xi Yao ◽  
...  
Keyword(s):  
Liquid Water ◽  
Molecular Level ◽  
Simulation Analysis ◽  
Antifreeze Proteins ◽  
Freezing Temperature ◽  
Ice Nucleation ◽  
Dynamics Simulation ◽  
Ice Binding ◽  
Solid Substrates ◽  
Unique Capability

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.

Protective role of antifreeze proteins on sterlet (Acipenser ruthenus) sperm during cryopreservation

2018 ◽  
Vol 44 (6) ◽  
pp. 1527-1533 ◽  
Author(s):  
Miaomiao Xin ◽  
Jan Sterba ◽  
Anna Shaliutina-Kolesova ◽  
Borys Dzyuba ◽  
Jaroslava Lieskovska ◽  
...  
Keyword(s):  
Antifreeze Proteins ◽  
Protective Role ◽  
Acipenser Ruthenus ◽  
Sterlet Acipenser Ruthenus

Multivalent Display of Antifreeze Proteins by Fusion to Self-Assembling Protein Cages Enhances Ice-Binding Activities

Biochemistry ◽  
2016 ◽  
Vol 55 (49) ◽  
pp. 6811-6820 ◽  
Author(s):  
Sean W. Phippen ◽  
Corey A. Stevens ◽  
Tyler D. R. Vance ◽  
Neil P. King ◽  
David Baker ◽  
...  
Keyword(s):  
Antifreeze Proteins ◽  
Protein Cages ◽  
Self Assembling ◽  
Ice Binding ◽  
Multivalent Display

Atomic Number Dependent “Structural Transitions” in Ordered Lanthanide Monolayers: Role of the Hydration Shell

Langmuir ◽  
2017 ◽  
Vol 33 (6) ◽  
pp. 1412-1418 ◽  
Author(s):  
Mitchell Miller ◽  
Miaoqi Chu ◽  
Binhua Lin ◽  
Wei Bu ◽  
Pulak Dutta
Keyword(s):  
Atomic Number ◽  
Hydration Shell ◽  
Structural Transitions

Role of the Solvation Water in Remote Interactions of Hyperactive Antifreeze Proteins with the Surface of Ice

2019 ◽  
Vol 123 (38) ◽  
pp. 8010-8018 ◽  
Author(s):  
Joanna Grabowska ◽  
Anna Kuffel ◽  
Jan Zielkiewicz
Keyword(s):  
Antifreeze Proteins
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