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New clues into the self-assembly of Vmh2, a basidiomycota class I hydrophobin

  • Anna Pennacchio , Paola Cicatiello , Eugenio Notomista , Paola Giardina EMAIL logo and Alessandra Piscitelli
Published/Copyright: June 20, 2018

Abstract

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.

Acknowledgments

The authors thank Dr. Alfredo Maria Gravagnuolo for the helpful discussions. This work was supported by a grant from the University Federico II, Naples, Italy (000023_ALTRI_DR_409_2017_Ricerca Ateneo_GIARDINA) ‘Immobilization of ENzymes on hydrophobin-functionalized NAnomaterials, IENA’.

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Supplementary Material:

The online version of this article offers supplementary material (https://doi.org/10.1515/hsz-2018-0124).


Received: 2018-01-16
Accepted: 2018-05-16
Published Online: 2018-06-20
Published in Print: 2018-07-26

©2018 Walter de Gruyter GmbH, Berlin/Boston

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