Fungal Hydrophobins and Their Self-Assembly into Functional Nanomaterials

被引:10
作者
Lo, Victor [1 ,2 ]
Lai, Jennifer I-Chun [1 ,2 ]
Sunde, Margaret [1 ,2 ]
机构
[1] Univ Sydney, Sch Med Sci, Fac Med & Hlth, Discipline Pharmacol, Sydney, NSW, Australia
[2] Sydney Nano, Sydney, NSW, Australia
来源
BIOLOGICAL AND BIO-INSPIRED NANOMATERIALS: PROPERTIES AND ASSEMBLY MECHANISMS | 2019年 / 1174卷
基金
澳大利亚研究理事会;
关键词
Hydrophobin; Self-assembly; Functional amyloid; Amphipathic; Surface active; Biomaterial; AIR-WATER-INTERFACE; CLASS-II HYDROPHOBINS; SCHIZOPHYLLUM-COMMUNE; INTRAVENOUS DELIVERY; CLADOSPORIUM-FULVUM; STRUCTURAL-ANALYSIS; TRICHODERMA-REESEI; CYS3-CYS4; LOOP; PROTEIN FILMS; RODLET LAYER;
D O I
10.1007/978-981-13-9791-2_5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In recent years, much attention has focused on incorporating biological and bio-inspired nanomaterials into various applications that range from functionalising surfaces and enhancing biomolecule binding properties, to coating drugs for improved bioavailability and delivery. Hydrophobin proteins, which can spontaneously assemble into amphipathic layers at hydrophobic:hydrophilic interfaces, are exciting candidates for use as nanomaterials. These unique proteins, which are only expressed by filamentous fungi, have been the focus of increasing interest from the biotechnology industry, as evidenced by the sharply growing number of hydrophobin-associated publications and patents. Here, we explore the contribution of different hydrophobins to supporting fungal growth and development. We describe the key structural elements of hydrophobins and the molecular characteristics that underlie self-assembly of these proteins at interfaces. We outline the multiple roles that hydrophobins can play in supporting aerial growth of filamentous structures, facilitating spore dispersal and preventing an immune response in the infected host. The growing understanding of the hydrophobin protein structure and self-assembly process highlights the potential for hydrophobin proteins to be engineered for use in a variety of novel applications that require biocompatible coatings.
引用
收藏
页码:161 / 185
页数:25
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