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Structure-Function Relationships in Hydrophobins: Probing the Role of Charged Side Chains

机译：疏水蛋白的结构-功能关系：探究带电侧链的作用

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Hydrophobins are small fungal proteins that are amphiphilic and have a strong tendency to assemble at interfaces. By taking advantage of this property, hydrophobins have been used for a number of applications: as affinity tags in protein purification, for protein immobilization, such as in foam stabilizers, and as dispersion agents for insoluble drug molecules. Here, we used site-directed mutagenesis to gain an understanding of the molecular basis of their properties. We especially focused on the role of charged amino acids in the structure of hydrophobins. For this purpose, fusion proteins consisting of Trichoderma reesei hydrophobin I (HFBI) and the green fluorescent protein (GFP) that contained various combinations of substitutions of charged amino acids (D30, K32, D40, D43, R45, K50) in the HFBI structure were produced. The effects of the introduced mutations on binding, oligomerization, and partitioning were characterized in an aqueous two-phase system. It was found that some substitutions caused better surface binding and reduced oligomerization, while some showed the opposite effects. However, all mutations decreased partitioning in surfactant systems, indicating that the different functions are not directly correlated and that partitioning is dependent on finely tuned properties of hydrophobins. This work shows that not all functions in self-assembly are connected in a predictable way and that a simple surfactant model for hydrophobin function is insufficient.
机译：疏水蛋白是两亲性的小真菌蛋白，具有在界面处聚集的强烈趋势。通过利用该特性，疏水蛋白已用于许多应用：作为蛋白质纯化中的亲和标签，用于蛋白质固定化（例如在泡沫稳定剂中）以及作为不溶性药物分子的分散剂。在这里，我们使用定点诱变来了解其特性的分子基础。我们特别关注带电荷氨基酸在疏水蛋白结构中的作用。为此，融合蛋白由里氏木霉疏水蛋白I（HFBI）和绿色荧光蛋白（GFP）组成，在HFBI结构中包含带电氨基酸取代的各种组合（D30，K32，D40，D43，R45，K50）被生产了。在水性两相系统中表征了引入的突变对结合，寡聚和分配的影响。发现一些取代引起更好的表面结合并减少了低聚，而另一些则显示相反的作用。但是，所有突变都减少了表面活性剂系统中的分配，表明不同的功能没有直接相关，并且分配取决于疏水蛋白的微调特性。这项工作表明，并不是所有的自组装功能都以可预测的方式连接，并且疏水蛋白功能的简单表面活性剂模型是不够的。

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