抗冻蛋白冰结合位点特征及其研究综述  

Review of characteristics of Ice-binding sites of antifreeze proteins

作　　者：杨如意 廖丽 胥义[1] YANG Ruyi;LIAO Li;XU Yi(School of Health Science and Engineering,University of Shanghai for Science and Technology,Shanghai 200093,China;Key Laboratory for Polar Science,Ministry of Natural Resources,Polar Research Institute of China,Shanghai 200136,China;School of Oceanography,Shanghai Jiao Tong University,Shanghai 200240,China)

机构地区：[1]上海理工大学健康科学与工程学院,上海200093 [2]自然资源部极地科学研究重点实验室,中国极地研究中心(中国极地研究所),上海200136 [3]上海交通大学海洋学院,上海200240

出　　处：《极地研究》2025年第1期137-148,共12页Chinese Journal of Polar Research

基　　金：国家自然科学基金(52076140);国家自然科学基金(41976224);国家重点研发计划(2022YFC2807501)资助。

摘　　要：冰结合位点(Ice-binding site,IBS)是抗冻蛋白(Antifreeze proteins,AFPs)与冰晶冰面结合、发挥抗冻作用的关键部分,对揭示AFPs调控冰晶成核的作用和机制十分重要。本文首先介绍了几种AFPs与冰结合机制及其IBS;其次,分别选取了动物、植物和微生物来源的AFPs,并对其IBS氨基酸序列及结构特征进行分析。结果表明,大多数AFPs的IBS都存在一个或多个重复的氨基酸序列与冰晶结合,而且这些氨基酸通常具有疏水性或者亲水性弱、侧链短等特点,使IBS相对疏水和平坦。一般而言,相同类型AFPs的IBS结构类似。AFP I的IBS氨基酸序列为TAA(A),Ca^(2+)依赖型AFP II的IBS均为DTTLTE,昆虫AFPs的IBS一般由TXT序列构成。微生物来源的AFPs可能因种属间差异大,IBS氨基酸序列、结构特征无明显规律。最后,归纳了2种IBS鉴定方法。氨基酸定点突变是IBS鉴定的主要方法,而分子模拟是对氨基酸定点突变的辅助验证。本文总结了不同类型AFPs的IBS规律,为AFPs IBS的比较研究及抗冻机制解析提供参考。Ice-binding sites represent critical regions in antifreeze proteins that interact with ice crystals,playing a pivotal role in their antifreeze function.They are essential for unraveling the regulatory roles and mechanisms of antifreeze proteins in ice crystal nucleation.This paper first introduces several models of antifreeze protein-ice binding,and then selects antifreeze proteins from animal,plant,and microbial sources to analyze their ice-binding sites amino acid sequences and structural characteristics.The results show that most antifreeze protein ice-binding sites have one or more repeated amino acid sequences that bind to ice crystals,and these amino acids are generally hydrophobic or have small hydrophilic groups and no long side chains,making the ice-binding sites relatively hydrophobic and flat.Generally speaking,the ice-binding site structure of the same type of antifreeze protein is similar.The amino acid sequence of AFP I’s ice-binding site is TAA(A),whereas Ca^(2+)-dependent AFP II’s ice-binding site is“DTTLTE”,and the ice-binding site of insect antifreeze proteins is generally composed of a“TXT”sequence.However,the amino acid sequence and structural characteristics of the ice-binding sites of antifreeze proteins from microbial sources may vary greatly due to species differences.Finally,two methods for identifying ice-binding sites are summarized.Typically,site-directed mutagenesis of amino acids serves as the primary approach for ice-binding site identification,with molecular simulations serving as auxiliary means to validate the effects of amino acid mutations.This review summarizes the patterns of ice-binding sites for different types of antifreeze proteins,providing a reference for comparative studies of antifreeze protein ice-binding sites and analysis of antifreeze mechanisms.

关 键 词：抗冻蛋白 冰结合位点 氨基酸突变 分子模拟 热滞活性 

分 类 号：Q51[生物学—生物化学]