Hydrophobin can prevent secondary protein adsorption on hydrophobic substrates without exchange |
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Authors: | Bernhard von Vacano Rui Xu Sabine Hirth Ines Herzenstiel Markus Rückel Thomas Subkowski Ulf Baus |
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Institution: | (1) Polymer Physics, BASF SE, Carl-Bosch-Str. 38, 67056 Ludwigshafen, Germany;(2) Biotechnology Research, BASF SE, Carl-Bosch-Str. 38, 67056 Ludwigshafen, Germany;(3) Performance Chemicals Division, BASF SE, Carl-Bosch-Str. 38, 67056 Ludwigshafen, Germany |
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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. |
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