A random sequential adsorption model for the irreversible binding of Tenebrio molitor antifreeze protein to ice crystals

被引：0

作者：

Guo, Tinghe ^{[1
]}

Zhang, Nan ^{[1
]}

Li, Yannan ^{[1
]}

Zhang, Luqiang ^{[1
]}

Wang, Jun ^{[1
]}

Zhang, Lirong ^{[1
]}

Liu, Junjie ^{[1
]}

机构：

[1] Inner Mongolia Univ, Sch Phys Sci & Technol, Inner Mongolia Key Lab Ion Beam Bioengn, Hohhot 010021, Peoples R China

来源：

AIP ADVANCES | 2024年 / 14卷 / 06期

基金：

中国国家自然科学基金;

关键词：

THERMAL HYSTERESIS; STRUCTURAL BASIS; ANNEALING TIME; INHIBITION; MECHANISM; INSECTS;

D O I：

10.1063/5.0212953

中图分类号：

TB3 [工程材料学];

学科分类号：

0805 ; 080502 ;

摘要：

A class of proteins known as antifreeze proteins (AFPs) appear in some organisms, allowing them to survive in low-temperature environments. These AFPs irreversibly adsorb to the surfaces of ice crystals and reduce the freezing temperature without significantly affecting the equilibrium melting point. Ice crystal growth is inhibited in the temperature gap between the melting point and the non-equilibrium freezing point, referred to as thermal hysteresis (TH). The irreversible adsorption of AFPs on the surfaces of ice crystals has been questioned because it is not consistent with the concentration dependence of the TH activity obtained from experimental studies. In this study, based on adsorption-inhibition theory, a random sequential adsorption model of AFPs was used to investigate the irreversible adsorption of hyperactive AFPs that have been found in the yellow mealworm beetle Tenebrio molitor (TmAFPs). The occupied fractions covered by TmAFP on ice crystal surfaces were obtained. The time and concentration dependence of the TH activity of TmAFP was analyzed. The theoretical results obtained from this model were consistent with reported experimental data. This work provides ideas and a theoretical basis for understanding the TH activity during the irreversible adsorption of AFPs.

引用

页数：8

共 39 条

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