A case study on biological activity in a surface-bound multicomponent system: The biotin-streptavidin-peroxidase system
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chair:
Chelmowski, R. / Prekelt, A. / Grunwald, C. / Wöll, C. (2008)
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place:
J. Phys. Chem. A (2008), 111, 12295-12303
- Date: 2008
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Chelmowski, R. / Prekelt, A. / Grunwald, C. / Wöll, C. (2008): „A case study on biological activity in a surface-bound multicomponent system: The biotin-streptavidin-peroxidase system“. In. J. Phys. Chem. A (2008), 111, 12295-12303
Abstract
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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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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