Structure-function relationships in hydrophobins: Probing the role of charged side chains

摘要: Hydrophobins are small fungal proteins that amphiphilic and have a strong tendency to assemble at interfaces. By taking advantage of this property, hydrophobins been used for number applications: as affinity tags in protein purification, immobilization, such foam stabilizers, dispersion agents insoluble drug molecules. Here, we site-directed mutagenesis gain an understanding the molecular basis their properties. We especially focused on role charged amino acids structure hydrophobins. For purpose, fusion consisting Trichoderma reesei hydrophobin I (HFBI) green fluorescent (GFP) contained various combinations substitutions (D30, K32, D40, D43, R45, K50) HFBI were produced. The effects introduced mutations binding, oligomerization, partitioning characterized aqueous two-phase system. It was found some caused better surface binding reduced while showed opposite effects. However, all decreased surfactant systems, indicating different functions not directly correlated is dependent finely tuned properties This work shows self-assembly connected predictable way simple model function insufficient.