Journal
BIOLOGICAL CHEMISTRY
Volume 399, Issue 8, Pages 895-901Publisher
WALTER DE GRUYTER GMBH
DOI: 10.1515/hsz-2018-0124
Keywords
3D model; amyloid fibrils; fibril formation; site-directed mutants; surface adhesion
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Funding
- University Federico II, Naples, Italy [000023_ALTRI_DR_409_2017_Ricerca Ateneo_GIARDINA]
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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 beta-hairpin, which in turn generates the beta-spine of the amyloid fibril.
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