%0 Journal Article
%A Gravagnuolo, Alfredo Maria
%A Longobardi, Sara
%A Luchini, Alessandra
%A Appavou, Marie-Sousai
%A De Stefano, Luca
%A Notomista, Eugenio
%A Paduano, Luigi
%A Giardina, Paola
%T Class I Hydrophobin Vmh2 Adopts Atypical Mechanisms to Self-Assemble into Functional Amyloid Fibrils
%J Biomacromolecules
%V 17
%N 3
%@ 1526-4602
%C Columbus, Ohio
%I American Chemical Soc.
%M FZJ-2016-06274
%P 954 - 964
%D 2016
%X Hydrophobins are fungal proteins whose functions are mainly based on their capability to self-assemble into amphiphilic films at hydrophobic–hydrophilic interfaces (HHI). It is widely accepted that class I hydrophobins form amyloid-like structures, named rodlets, which are hundreds of nanometers long, packed into ordered lateral assemblies and do not exhibit an overall helical structure. We studied the self-assembly of the Class I hydrophobin Vmh2 from Pleurotus ostreatus in aqueous solutions by dynamic light scattering (DLS), thioflavin T (ThT), fluorescence assay, circular dichroism (CD), cryogenic trasmission electron microscopy (cryo-TEM), and TEM. Vmh2 does not form fibrillar aggregates at HHI. It exhibits spherical and fibrillar assemblies whose ratio depends on the protein concentration when freshly solubilized at pH ≥ 7. Moreover, it spontaneously self-assembles into isolated, micrometer long, and twisted amyloid fibrils, observed for the first time in fungal hydrophobins. This process is promoted by acidic pH, temperature, and Ca2+ ions. A model of self-assembly into amyloid-like structures has been proposed.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000372391800027
%$ pmid:26828412
%R 10.1021/acs.biomac.5b01632
%U https://juser.fz-juelich.de/record/821017