Department of Chemical Sciences, University of Naples "Federico II", via Cintia 4, I-80126 Naples, Italy.
Department of Biology, University of Naples "Federico II", Via Cintia 4, I-80126 Naples, Italy.
Biol Chem. 2018 Jul 26;399(8):895-901. doi: 10.1515/hsz-2018-0124.
Hydrophobins are fungal proteins that can self-assemble into amphiphilic films at hydrophobic-hydrophilic interfaces. Class I hydrophobin aggregates resemble amyloid fibrils, sharing some features with them. Here, five site-directed mutants of Vmh2, a member of basidiomycota class I hydrophobins, were designed and characterized to elucidate the molecular determinants playing a key role in class I hydrophobin self-assembly. The mechanism of fibril formation proposed for Vmh2 foresees that the triggering event is the destabilization of a specific loop (L1), leading to the formation of a β-hairpin, which in turn generates the β-spine of the amyloid fibril.
水蛋白是一类真菌蛋白，能够在疏水-亲水界面上自组装成两亲性薄膜。I 类水蛋白聚集体类似于淀粉样纤维，与它们具有一些共同特征。在此，设计并表征了 5 种来源于担子菌纲 I 类水蛋白的 Vmh2 定点突变体，以阐明在 I 类水蛋白自组装中起关键作用的分子决定因素。提出的 Vmh2 纤维形成机制设想，触发事件是特定环（L1）的去稳定化，导致β发夹的形成，进而产生淀粉样纤维的β-棘。
