期刊
ANALYTICAL AND BIOANALYTICAL CHEMISTRY
卷 400, 期 7, 页码 2031-2040出版社
SPRINGER HEIDELBERG
DOI: 10.1007/s00216-011-4902-x
关键词
Hydrophobin; Protein adsorption; Secondary ion mass spectrometry; Quartz-crystal microbalance; X-ray photoelectron spectroscopy
资金
- DAAD (German Academic Exchange Service)
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据