Computational Assessment of Modified Antifreeze Glycoproteins on Ice Nucleation

Biophysica

Matt Reil¹  Monika Bleszynski¹ 

[1] Department of Mechanical & Materials Engineering, Ritchie School of Engineering and Computer Science, University of Denver, Denver, CO 80208, USA;

关键词: antifreeze glycoproteins;    molecular dynamics;    ice nucleation;    hydroxyl group separation distance;   

DOI  :  10.3390/biophysica1020013

来源: DOAJ

【 摘 要 】

Antifreeze glycoproteins (AFGPs) found in various fish are used by the organisms to prevent freezing. While these compounds have been studied for their ability to bind to, and prevent the complete crystallization of water, the exact mechanisms by which AFGPs prevent freezing are still undetermined. Therefore, building upon our previous work, this study uses molecular dynamics simulations to assess the effects of hydroxyl group separation distance on AFGP ice nucleation activity. Water droplet crystallization simulations showed that modified AFGP structures containing hydroxyl distances smaller than ~3.0 Å lost their ability to prevent ice crystallization. Furthermore, modified AFGP containing hydroxyl distances of 7.327 Å and 6.160 Å was correlated with a promotion in ice nucleation, as demonstrated by the changes in the energy of the system. This supports the notion that the distance, and therefore, geometry characteristics between the hydroxyl groups located on the saccharide structures play a key role in the ice crystallization inhibition properties of AFGP compounds.

【 授权许可】

Unknown