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| 001 | 821017 | ||
| 005 | 20240619091216.0 | ||
| 024 | 7 | _ | |a 10.1021/acs.biomac.5b01632 |2 doi |
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| 100 | 1 | _ | |a Gravagnuolo, Alfredo Maria |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Class I Hydrophobin Vmh2 Adopts Atypical Mechanisms to Self-Assemble into Functional Amyloid Fibrils |
| 260 | _ | _ | |a Columbus, Ohio |c 2016 |b American Chemical Soc. |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a 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. |
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| 700 | 1 | _ | |a Longobardi, Sara |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Luchini, Alessandra |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Appavou, Marie-Sousai |0 P:(DE-Juel1)130507 |b 3 |u fzj |
| 700 | 1 | _ | |a De Stefano, Luca |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Notomista, Eugenio |0 P:(DE-HGF)0 |b 5 |
| 700 | 1 | _ | |a Paduano, Luigi |0 P:(DE-HGF)0 |b 6 |
| 700 | 1 | _ | |a Giardina, Paola |0 P:(DE-HGF)0 |b 7 |e Corresponding author |
| 773 | _ | _ | |a 10.1021/acs.biomac.5b01632 |g Vol. 17, no. 3, p. 954 - 964 |0 PERI:(DE-600)2006291-6 |n 3 |p 954 - 964 |t Biomacromolecules |v 17 |y 2016 |x 1526-4602 |
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