title: Environmental conditions modulate the switch among different states of the hydrophobin Vmh2 from Pleurotus ostreatus.
abstract: Fungal hydrophobins are amphipathic, highly surface-active, and self-assembling proteins. The class I hydrophobin Vmh2 from the basidiomycete fungus  Pleurotus ostreatus  seems to be the most hydrophobic hydrophobin characterized so far. Structural and functional properties of the protein as a function of the environmental conditions have been determined. At least three distinct phenomena can occur, being modulated by the environmental conditions: (1) when the pH increases or in the presence of Ca(2+) ions, an assembled state, β-sheet rich, is formed; (2) when the solvent polarity increases, the protein shows an increased tendency to reach hydrophobic/hydrophilic interfaces, with no detectable conformational change; and (3) when a reversible conformational change and reversible aggregation occur at high temperature. Modulation of the Vmh2 conformational/aggregation features by changing the environmental conditions can be very useful in view of the potential protein applications.
authors.affiliation: Department of Organic Chemistry and Biochemistry, University of Naples Federico II, Naples, Italy.
authors.forename: Sara
authors.initials: S
authors.lastname: Longobardi
authors.forename: Delia
authors.initials: D
authors.lastname: Picone
authors.forename: Carmine
authors.initials: C
authors.lastname: Ercole
authors.forename: Roberta
authors.initials: R
authors.lastname: Spadaccini
authors.forename: Luca
authors.initials: L
authors.lastname: De Stefano
authors.forename: Ilaria
authors.initials: I
authors.lastname: Rea
authors.forename: Paola
authors.initials: P
authors.lastname: Giardina
mesh_terms: D000682:Amyloid / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D004777:Environment; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D020076:Pleurotus / Q000378:metabolism; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012997:Solvents / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D000682:Amyloid; D005656:Fungal Proteins; D011994:Recombinant Proteins; D012997:Solvents; D002118:Calcium