Protein adsorption on tailored substrates:: long-range forces and conformational changes

被引：51

作者：

Bellion, M. ^{[1
]}

Santen, L. ^{[1
]}

Mantz, H. ^{[2
]}

Haehl, H. ^{[2
]}

Quinn, A. ^{[2
]}

Nagel, A. ^{[2
]}

Gilow, C. ^{[2
]}

Weitenberg, C. ^{[2
]}

Schmitt, Y. ^{[2
]}

Jacobs, K. ^{[2
]}

机构：

[1] Univ Saarland, Dept Theoret Phys, D-66041 Saarbrucken, Germany

[2] Univ Saarland, Dept Expt Phys, D-66041 Saarbrucken, Germany

来源：

JOURNAL OF PHYSICS-CONDENSED MATTER | 2008年 / 20卷 / 40期

关键词：

D O I：

10.1088/0953-8984/20/40/404226

中图分类号：

O469 [凝聚态物理学];

学科分类号：

070205 ;

摘要：

Adsorption of proteins onto solid surfaces is an everyday phenomenon that is not yet fully understood. To further the current understanding, we have performed in situ ellipsometry studies to reveal the adsorption kinetics of three different proteins, lysozyme, alpha-amylase and bovine serum albumin. As substrates we offer Si wafers with a controlled Si oxide layer thickness and a hydrophilic or hydrophobic surface functionalization, allowing the tailoring of the influence of short- and long-range interactions. Our studies show that not only the surface chemistry determines the properties of an adsorbed protein layer but also the van der Waals contributions of a composite substrate. We compare the experimental findings to results of a colloidal Monte Carlo approach that includes conformational changes of the adsorbed proteins induced by density fluctuations.

引用

页数：11

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