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 Ca2+ ions, an assembled state, -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; 3- a reversible conformational change and reversible aggregation occurs 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.

Environmental conditions modulate the switch among different states of the hydrophobin Vmh2 from Pleurotus ostreatus

LONGOBARDI, SARA;PICONE, DELIA;ERCOLE, CARMINE;REA, ILARIA;GIARDINA, PAOLA
2012

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 Ca2+ ions, an assembled state, -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; 3- a reversible conformational change and reversible aggregation occurs 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.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/426934
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