Hyperactive Antifreeze Proteins Promote Ice Growth before Binding to It

Author(s):  
Shaoli Cui ◽  
Weijia Zhang ◽  
Xueguang Shao ◽  
Wensheng Cai
2020 ◽  
Author(s):  
Jinzi Deng ◽  
Elana Apfelbaum ◽  
Ran Drori

<p>Since some antifreeze proteins and glycoproteins (AF(G)Ps) cannot directly bind to all crystal planes, they change ice crystal morphology by minimizing the area of the crystal planes to which they cannot bind until crystal growth is halted. Previous studies found that growth along the <i>c</i>-axis (perpendicular to the basal plane, the crystal plane to which these AF(G)Ps cannot bind) is accelerated by some AF(G)Ps, while growth of other planes is inhibited. The effects of this growth acceleration on crystal morphology and on the thermal hysteresis activity are unknown to date. Understanding these effects will elucidate the mechanism of ice growth inhibition by AF(G)Ps. Using cold stages and an Infrared laser, ice growth velocities and crystal morphologies in AF(G)P solutions were measured. Three types of effects on growth velocity were found: concentration-dependent acceleration, concentration-independent acceleration, and concentration-dependent deceleration. Quantitative crystal morphology measurements in AF(G)P solutions demonstrated that adsorption rate of the proteins to ice plays a major role in determining the morphology of the bipyramidal crystal. These results demonstrate that faster adsorption rates generate bipyramidal crystals with diminished basal surfaces at higher temperatures compared to slower adsorption rates. The acceleration of growth along the <i>c</i>-axis generates crystals with smaller basal surfaces at higher temperatures leading to increased growth inhibition of the entire crystal.<a></a></p>


2020 ◽  
Vol 8 (44) ◽  
pp. 23555-23562
Author(s):  
Xing Liu ◽  
Hongya Geng ◽  
Nan Sheng ◽  
Jianjun Wang ◽  
Guosheng Shi

Design of biomimetic two-dimensional graphene derivatives to suppress ice crystal growth.


2003 ◽  
Vol 81 (1-2) ◽  
pp. 39-45 ◽  
Author(s):  
B Wathen ◽  
M J Kuiper ◽  
V K Walker ◽  
Z Jia

A Monte Carlo computational method for simulating the growth of entire ice crystals from the liquid phase has been developed specifically to study the inhibition of ice-crystal growth by antifreeze proteins (AFPs). AFPs are found in the fluids of certain organisms that inhabit freezing environments and constrain ice-crystal growth by adsorbtion to the ice surface, but their inhibition mechanism is still poorly understood. Thus, it was of interest to incorporate these molecules into the dynamic ice simulations to examine the inhibition phenomenon on a whole-crystal basis. We have undertaken simulations with AFPs from two different organisms that differ in activity; the insect AFP has up to 100 times the activity of the fish AFP on a molar basis. Simulations involving insect and fish AFPs have achieved ice-growth inhibition at simulation temperatures within reported activity ranges for both fish and insect AFPs, accompanied by resulting ice morphologies similar to those observed experimentally. These results, as well as other studies on ice-etching patterns and ice burst growth at temperatures below known AFP ice-growth inhibition abilities suggest that AFP activity is dominated by the AFP ice-binding position rather than AFP ice-binding strength. PACS No.: 07.05T


Langmuir ◽  
2015 ◽  
Vol 31 (21) ◽  
pp. 5805-5811 ◽  
Author(s):  
Ran Drori ◽  
Peter L. Davies ◽  
Ido Braslavsky

2020 ◽  
Author(s):  
Jinzi Deng ◽  
Elana Apfelbaum ◽  
Ran Drori

<p>Since some antifreeze proteins and glycoproteins (AF(G)Ps) cannot directly bind to all crystal planes, they change ice crystal morphology by minimizing the area of the crystal planes to which they cannot bind until crystal growth is halted. Previous studies found that growth along the <i>c</i>-axis (perpendicular to the basal plane, the crystal plane to which these AF(G)Ps cannot bind) is accelerated by some AF(G)Ps, while growth of other planes is inhibited. The effects of this growth acceleration on crystal morphology and on the thermal hysteresis activity are unknown to date. Understanding these effects will elucidate the mechanism of ice growth inhibition by AF(G)Ps. Using cold stages and an Infrared laser, ice growth velocities and crystal morphologies in AF(G)P solutions were measured. Three types of effects on growth velocity were found: concentration-dependent acceleration, concentration-independent acceleration, and concentration-dependent deceleration. Quantitative crystal morphology measurements in AF(G)P solutions demonstrated that adsorption rate of the proteins to ice plays a major role in determining the morphology of the bipyramidal crystal. These results demonstrate that faster adsorption rates generate bipyramidal crystals with diminished basal surfaces at higher temperatures compared to slower adsorption rates. The acceleration of growth along the <i>c</i>-axis generates crystals with smaller basal surfaces at higher temperatures leading to increased growth inhibition of the entire crystal.<a></a></p>


2019 ◽  
Vol 10 (23) ◽  
pp. 2986-2990 ◽  
Author(s):  
Laura E. Wilkins ◽  
Muhammad Hasan ◽  
Alice E. R. Fayter ◽  
Caroline Biggs ◽  
Marc Walker ◽  
...  

Antifreeze proteins are site-specifically conjugated onto polymer-stabilised gold nanoparticles, resulting in hybrid materials capable of modulating ice growth processes.


2019 ◽  
Vol 10 (5) ◽  
pp. 966-972 ◽  
Author(s):  
Lukas Eickhoff ◽  
Katharina Dreischmeier ◽  
Assaf Zipori ◽  
Vera Sirotinskaya ◽  
Chen Adar ◽  
...  

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