A case study on biological activity in a surface-bound multicomponent system:: The biotin-streptavidin-peroxidase system

被引：19

作者：

Chelmowski, Rolf ^{[1
]}

Prekelt, Andreas ^{[1
]}

Grunwald, Christian ^{[1
]}

Woell, Christof ^{[1
]}

机构：

[1] Ruhr Univ Bochum, D-44780 Bochum, Germany

来源：

JOURNAL OF PHYSICAL CHEMISTRY A | 2007年 / 111卷 / 49期

关键词：

D O I：

10.1021/jp074847u

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The adsorption of multiple protein layers on biotinylated organic surfaces has been characterized using surface plasmon resonance (SPR) and atomic force microscopy (AFM). Diffusion-limited loading of the biotinylated self-assembled monolayers (SAMs) ensures a precise control of the streptavidin surface density. For the subsequent interaction with biotinylated peroxidase, SPR data hint at a streptavidin density dependent orientation during peroxidase adsorption. Microcontact printed well-defined two-dimensional patterned surfaces of biotinylated organothiols and protein-resistant OEG-thiols allow an in-situ differentiation of specific and nonspecific adsorption (e.g., mono- vs multilayer adsorption). Additionally, the very important issue of biological activity of surface-bound enzymes is addressed by comparing the enzyme activities in solution with that for surface-bound species.

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收藏

页码：12295 / 12303

页数：9

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