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

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.

scholarly journals Nanoscale assemblies and their biomedical applications

2013 ◽  
Vol 10 (80) ◽  
pp. 20120740 ◽  
Author(s):  
Tais A. P. F. Doll ◽  
Senthilkumar Raman ◽  
Raja Dey ◽  
Peter Burkhard
Keyword(s):  
Biomedical Applications ◽  
Vaccine Development ◽  
Building Blocks ◽  
Eukaryotic Cells ◽  
Peptide Nanotubes ◽  
Protein Cages ◽  
Bacterial Microcompartments ◽  
Self Assembling ◽  
Development Section ◽  
Characteristic Features

Nanoscale assemblies are a unique class of materials, which can be synthesized from inorganic, polymeric or biological building blocks. The multitude of applications of this class of materials ranges from solar and electrical to uses in food, cosmetics and medicine. In this review, we initially highlight characteristic features of polymeric nanoscale assemblies as well as those built from biological units (lipids, nucleic acids and proteins). We give special consideration to protein nanoassemblies found in nature such as ferritin protein cages, bacterial microcompartments and vaults found in eukaryotic cells and designed protein nanoassemblies, such as peptide nanofibres and peptide nanotubes. Next, we focus on biomedical applications of these nanoscale assemblies, such as cell targeting, drug delivery, bioimaging and vaccine development. In the vaccine development section, we report in more detail the use of virus-like particles and self-assembling polypeptide nanoparticles as new vaccine delivery platforms.

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

Understanding the mechanism of ice binding by type III antifreeze proteins

2001 ◽  
Vol 305 (4) ◽  
pp. 875-889 ◽  
Author(s):  
Alfred A. Antson ◽  
Derek J. Smith ◽  
David I. Roper ◽  
Sally Lewis ◽  
Leo S.D. Caves ◽  
...  
Keyword(s):  
Antifreeze Proteins ◽  
Type Iii ◽  
Ice Binding

scholarly journals Ice-binding site of surface-bound type III antifreeze protein partially decoupled from water

2018 ◽  
Vol 20 (42) ◽  
pp. 26926-26933 ◽  
Author(s):  
Dominique Verreault ◽  
Sarah Alamdari ◽  
Steven J. Roeters ◽  
Ravindra Pandey ◽  
Jim Pfaendtner ◽  
...  
Keyword(s):  
Binding Site ◽  
Antifreeze Proteins ◽  
Antifreeze Protein ◽  
Water Interface ◽  
Native State ◽  
Type Iii ◽  
Ice Binding ◽  
Air Water Interface

Combined SFG/MD analysis together with spectral calculations revealed that type III antifreeze proteins adsorbed at the air–water interface maintains a native state and adopts an orientation that leads to a partial decoupling of its ice-binding site from water.

scholarly journals Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity

10.3791/51185 ◽  
2014 ◽  
Author(s):  
Koli Basu ◽  
Christopher P. Garnham ◽  
Yoshiyuki Nishimiya ◽  
Sakae Tsuda ◽  
Ido Braslavsky ◽  
...  
Keyword(s):  
Antifreeze Proteins ◽  
Ice Binding
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