title: The SC3 hydrophobin self-assembles into a membrane with distinct mass transfer properties.
abstract: Hydrophobins are a class of small proteins that fulfill a wide spectrum of functions in fungal growth and development. They do so by self-assembling into an amphipathic membrane at hydrophilic-hydrophobic interfaces. The SC3 hydrophobin of Schizophyllum commune is the best-studied hydrophobin. It assembles at the air-water interface into a membrane consisting of functional amyloid fibrils that are called rodlets. Here we examine the dynamics of SC3 assembly at an oil-water and air-water interface and the permeability characteristics of the assembled layer. Hydrophobin assembled at an oil-water interface is a dynamic system capable of emulsifying oil. It accepts soluble-state SC3 oligomers from water in a unidirectional process and sloughs off SC3 vesicles back into the water phase enclosing a portion of the oil phase in their hydrophobic interior. The assembled layer is impermeable to solutes >200 Da from either the water phase or the oil phase; however, due to the emulsification process, oil and the hydrophobic marker molecules in the oil phase can be transferred into the water phase, thus giving the impression that the assembled layer is permeable to the marker molecules. By contrast, the layer assembled at an air-water interface is permeable to water vapor from either the hydrophobic or hydrophilic side.
authors.affiliation: Biomade Technology Foundation, Groningen, The Netherlands.
authors.forename: X
authors.initials: X
authors.lastname: Wang
authors.forename: Fuxin
authors.initials: F
authors.lastname: Shi
authors.forename: H A B
authors.initials: HA
authors.lastname: Wösten
authors.forename: H
authors.initials: H
authors.lastname: Hektor
authors.forename: B
authors.initials: B
authors.lastname: Poolman
authors.forename: G T
authors.initials: GT
authors.lastname: Robillard
mesh_terms: D000388:Air; D016229:Amyloid beta-Peptides / Q000737:chemistry; D052160:Benzothiazoles; D001703:Biophysics / Q000379:methods*; D005656:Fungal Proteins / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry; D008566:Membranes / Q000737:chemistry* / Q000378:metabolism; D018613:Microscopy, Confocal; D008856:Microscopy, Fluorescence; D017830:Octoxynol / Q000494:pharmacology; D009821:Oils / Q000737:chemistry; D010232:Paraffin; D010539:Permeability; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012567:Schizophyllum / Q000378:metabolism; D013844:Thiazoles / Q000737:chemistry*; D013997:Time Factors; D014867:Water / Q000737:chemistry
chemical_list: D016229:Amyloid beta-Peptides; D052160:Benzothiazoles; D005656:Fungal Proteins; D008565:Membrane Proteins; D009821:Oils; D013844:Thiazoles; D014867:Water; C009462:thioflavin T; D010232:Paraffin; D017830:Octoxynol