TY  - JOUR
AU  - Gravagnuolo, Alfredo Maria
AU  - Longobardi, Sara
AU  - Luchini, Alessandra
AU  - Appavou, Marie-Sousai
AU  - De Stefano, Luca
AU  - Notomista, Eugenio
AU  - Paduano, Luigi
AU  - Giardina, Paola
TI  - Class I Hydrophobin Vmh2 Adopts Atypical Mechanisms to Self-Assemble into Functional Amyloid Fibrils
JO  - Biomacromolecules
VL  - 17
IS  - 3
SN  - 1526-4602
CY  - Columbus, Ohio
PB  - American Chemical Soc.
M1  - FZJ-2016-06274
SP  - 954 - 964
PY  - 2016
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000372391800027
C6  - pmid:26828412
DO  - DOI:10.1021/acs.biomac.5b01632
UR  - https://juser.fz-juelich.de/record/821017
ER  -