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.Fig. 1The combination of surface analytical methods shows that an adsorbed layer of H*Protein B, a technically available representative of the hydrophobin family, prevents adsorption of secondary proteins at low-salinity conditions and pH 8. Due to the multi-method approach it can be proven that no exchange of the adsorbed hydrophobin protein is taking place

The Arthroderma benhamiae Hydrophobin HypA Mediates Hydrophobicity and Influences Recognition by Human Immune Effector Cells

“…The aggregates formed are of interest for both material science and biotechnology. Moreover, since the RodA hydrophobin of A. fumigatus has been shown to render surfaces immunologically inert and prevent the adsorption of other proteins onto hydrophobin-covered surfaces (1,39), it is the aim of research projects to establish long-term stable protective layers by using fungal hydrophobins. For conidia of dermatophytes, a rodlet layer was described in the 1970s.…”

Applications of hydrophobins: current state and perspectives

“…Depending on the hydrophobin used and environmental conditions such as pH and ionic strength, differential binding and/or antifouling properties can be obtained. An adsorbed layer of H*Protein B on octanethiol-coated gold prevented the adsorption of the secondary proteins BSA, casein, and collagen at low-salinity conditions and at pH 8 (von Vacano et al 2011). Surface analysis showed that the hydrophobin layer stays intact during several hours of exposure to solutions of secondary proteins without any detectable exchange with these proteins.…”

Hydrophobins as aqueous lubricant additive for a soft sliding contact

“…Surface-active properties of hydrophobins have drawn particular interests in self-assembled adsorption behavior of hydrophobins at air/water [8][9][10], water/oil [11][12][13][14], and water/solid interfaces [15][16][17][18][19][20][21][22]. This, in turn, sparked intensive researches to utilize hydrophobins as coating materials for biomedical, technical, and personal care products [23][24][25][26][27][28].…”