Hydrophobin can prevent secondary protein adsorption on hydrophobic substrates without exchange
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- 作者：Bernhard von Vacano (1) bernhard.von-vacano@basf.com
Rui Xu (1)
Sabine Hirth (1)
Ines Herzenstiel (1)
Markus R眉ckel (1)
Thomas Subkowski (2)
Ulf Baus (3) - 关键词：Hydrophobin – ; Protein adsorption – ; Secondary ion mass spectrometry – ; Quartz ; crystal microbalance – ; X ; ray photoelectron spectroscopy
- 刊名：Analytical and Bioanalytical Chemistry
- 出版时间：June 2011
- 出版年：2011
- 期刊代码：8_1618-2642
- 类别：en
- 卷：400
- 期：7
- 页码：2031-2040
- 数据来源：sp
摘要
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.