Understanding and engineering hydrophobin self-assembly

了解和设计疏水蛋白自组装

• 批准号: RGPIN-2017-05338
• 负责人: Langelaan, David
• 金额: $ 1.89万
• 依托单位: Dalhousie University
• 依托单位国家: 加拿大
• 项目类别: Discovery Grants Program - Individual
• 财政年份: 2020
• 资助国家: 加拿大
• 起止时间: 2020-01-01 至 2021-12-31
• 项目状态: 已结题
• 来源: https://www.nserc-crsng.gc.ca/ase-oro/Details-Detailles_eng.asp?id=710154
• 关键词: Understanding; engineering; hydrophobin; self; assembly

Protein self-assembly plays many essential roles in nature and presents new opportunities to develop biomaterials. One family of self-assembling proteins are hydrophobins, which are small globular proteins produced by filamentous fungi to modify their environment. Secreted hydrophobins behave like detergents and can change shape to form rodlets, which are an extremely durable and water repellent coating over aerial hyphae and spores. The unusual biochemical properties of hydrophobins have generated interest in developing them for commercial applications as emulsifiers, foam stabilizers and as an agent to protect and modify surfaces. Currently a comprehensive, molecular-based understanding of the properties of hydrophobins and how they form rodlets is lacking. Only a handful of high-resolution structures for hydrophobins exist, but these are for hydrophobins so diverse in sequence and structure that it is difficult to correlate the sequence and structural properties of these hydrophobins with their function. In collaboration with Dr. Emma Master (UofT) I have begun to characterize the structure and function of a new sub-class of hydrophobins. By studying these hydrophobins I will correlate sequence features of hydrophobins with their functional properties. Specifically, the objectives of this proposal are to: 1. Characterize the structure and function of diverse hydrophobins and determine what factors influence their properties. 2. Determine how rodlet formation occurs and build a working model of the rodlet structure. 3. Design hydrophobins that assemble into rodlets with desired properties. To address these objectives I will use an experimental approach combining molecular biology, structural biology, and biophysics. This work will contribute to our knowledge of protein self-assembly and will provide a mechanistic understanding of hydrophobin properties and function that is critical to engineer them for commercial applications. My research program will allow trainees to develop skills in molecular biology, nuclear magnetic resonance spectroscopy, X-ray crystallography, circular dichroism spectropolarimetry, atomic force microscopy, and electron microscopy. These diverse skills and and experience working with a protein that is currently being developed for commercialization will ensure the success of highly qualified personnel in their future careers in the biotechnology, pharmaceutical and academic sectors.

蛋白质自组装在自然界中发挥着重要作用，为生物材料的开发提供了新的机遇。一类自组装蛋白是疏水蛋白，它是丝状真菌为改变环境而产生的小球状蛋白。分泌的疏水蛋白就像清洁剂一样，可以改变形状形成小棒，这是一种非常耐用和防水的涂层，覆盖在空气中的菌丝和孢子上。疏水性化合物的不同寻常的生化特性引起了人们对开发它们作为乳化剂、泡沫稳定剂和保护和修饰表面的剂的商业应用的兴趣。