真菌疏水蛋白结构研究进展

Research Progress on the Structural Analysis of Hydrophobins

真菌疏水蛋白是由高等丝状真菌产生的小分子量(10kD左右)具有双亲性的蛋白质,它们在真菌生长和发育中起着重要的作用。通过研究发现疏水蛋白具有极高的表面活性,可以在界面通过自组装形成双亲性的蛋白膜,从而改变界面的亲疏水性质。值得注意的是,疏水蛋白的不同功能可归因于其双亲性蛋白质结构,使得其在不同的亲水/疏水界面处自组装以形成两性蛋白膜。基于这样的性质,疏水蛋白已经获得了国内外各领域的广泛应用。疏水蛋白潜在的应用价值激励了人们对其蛋白结构的探究从而解释其自组装机理。此篇综述总结了近些年人们通过不同手段及研究方法来解释疏水蛋白发挥功能的结构基础。

Hydrophobin is a type of small-secreted amphiphilic proteins(about 10 kD)produced by filamentous fungi and they play important roles in fungal growth and development.It is found that the hydrophobin has extremely high surface activity,and can form the amphiphilic protein membrane by self-assembly at the interface,thus changing the wettability of the interface.Notably,these diverse functions of hydrophobins can be attributed to their amphiphilic protein structures,resulting in their self-assembly at different hydrophilic/hydrophobic interfaces to form an amphipathic protein film.Based on such a property,hydrophobins have obtained various applications.The potential application value of hydrophobin has motivated people to explore its structural mechanism of self-assembly.This review summarizes the structural basis for the interpretation of hydrophobin’s function through different means and research methods in recent years.