title: Hydrophobin can prevent secondary protein adsorption on hydrophobic substrates without exchange.
abstract: By combining several surface analytical tools, we show that an adsorbed layer of the protein H*Protein B prevents the adsorption of secondary proteins bovine serum albumin, casein, or collagen at low-salinity conditions and at pH 8. H*Protein B is an industrially producible fusion protein of the hydrophobin family, known for its high interfacial activity. While applications of hydrophobin have been reported to facilitate adhesion of proteins under different pH conditions, careful analysis by quartz-crystal microbalance and ellipsometry prove that no additional adsorption can be found on top of the H*Protein B layer in this study. Surface analysis by X-ray photoelectron spectroscopy and secondary ion mass spectrometry proves that the hydrophobin layer stays intact even after hours of exposure to solutions of the secondary proteins and that no exchange of proteins can be detected.
authors.affiliation: Polymer Physics, BASF SE, Carl-Bosch-Str. 38, 67056, Ludwigshafen, Germany. bernhard.von-vacano@basf.com
authors.forename: Bernhard
authors.initials: B
authors.lastname: von Vacano
authors.forename: Rui
authors.initials: R
authors.lastname: Xu
authors.forename: Sabine
authors.initials: S
authors.lastname: Hirth
authors.forename: Ines
authors.initials: I
authors.lastname: Herzenstiel
authors.forename: Markus
authors.initials: M
authors.lastname: Rückel
authors.forename: Thomas
authors.initials: T
authors.lastname: Subkowski
authors.forename: Ulf
authors.initials: U
authors.lastname: Baus
mesh_terms: D000327:Adsorption; D011506:Proteins / Q000737:chemistry*; D013057:Spectrum Analysis; D013499:Surface Properties; D014965:X-Rays
chemical_list: D011506:Proteins