Sunde Margaret, Kwan Ann H Y, Templeton Matthew D, Beever Ross E, Mackay Joel P
School of Molecular and Microbial Biosciences, University of Sydney, Sydney 2006, Australia.
Micron. 2008 Oct;39(7):773-84. doi: 10.1016/j.micron.2007.08.003. Epub 2007 Aug 10.
Hydrophobins are a remarkable class of small cysteine-rich proteins found exclusively in fungi. They self-assemble to form robust polymeric monolayers that are highly amphipathic and play numerous roles in fungal biology, such as in the formation and dispersal of aerial spores and in pathogenic and mutualistic interactions. The polymeric form can be reversibly disassembled and is able to reverse the wettability of a surface, leading to many proposals for nanotechnological applications over recent years. The surprising properties of hydrophobins and their potential for commercialization have led to substantial efforts to delineate their morphology and molecular structure. In this review, we summarize the progress that has been made using a variety of spectroscopic and microscopic approaches towards understanding the molecular mechanisms underlying hydrophobin structure.
疏水蛋白是一类仅在真菌中发现的、富含半胱氨酸的特殊小分子蛋白质。它们能够自我组装形成坚固的聚合物单分子层，这种单分子层具有高度的两亲性，在真菌生物学中发挥着多种作用，例如在气生孢子的形成和传播以及致病性和共生相互作用中。聚合物形式可以可逆地分解，并能够改变表面的润湿性，这使得近年来人们对其在纳米技术应用方面提出了许多设想。疏水蛋白令人惊讶的特性及其商业化潜力促使人们付出了巨大努力来描绘它们的形态和分子结构。在这篇综述中，我们总结了使用各种光谱和显微镜方法在理解疏水蛋白结构背后的分子机制方面所取得的进展。
