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000821017 1001_ $$0P:(DE-HGF)0$$aGravagnuolo, Alfredo Maria$$b0
000821017 245__ $$aClass I Hydrophobin Vmh2 Adopts Atypical Mechanisms to Self-Assemble into Functional Amyloid Fibrils
000821017 260__ $$aColumbus, Ohio$$bAmerican Chemical Soc.$$c2016
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000821017 520__ $$aHydrophobins 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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000821017 7001_ $$0P:(DE-HGF)0$$aLongobardi, Sara$$b1
000821017 7001_ $$0P:(DE-HGF)0$$aLuchini, Alessandra$$b2
000821017 7001_ $$0P:(DE-Juel1)130507$$aAppavou, Marie-Sousai$$b3$$ufzj
000821017 7001_ $$0P:(DE-HGF)0$$aDe Stefano, Luca$$b4
000821017 7001_ $$0P:(DE-HGF)0$$aNotomista, Eugenio$$b5
000821017 7001_ $$0P:(DE-HGF)0$$aPaduano, Luigi$$b6
000821017 7001_ $$0P:(DE-HGF)0$$aGiardina, Paola$$b7$$eCorresponding author
000821017 773__ $$0PERI:(DE-600)2006291-6$$a10.1021/acs.biomac.5b01632$$gVol. 17, no. 3, p. 954 - 964$$n3$$p954 - 964$$tBiomacromolecules$$v17$$x1526-4602$$y2016
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