On-line detection of nonspecific protein adsorption at artificial surfaces

Seigel, R. Ros; Harder, P.; Dahint, R.; Grunze, M.; Josse, F.; Mrksich, M.; Whitesides, G.M.

doi:10.1021/ac970047b

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On-line detection of nonspecific protein adsorption at artificial surfaces

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Grunze, M.
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Seigel, R. R., Harder, P., Dahint, R., Grunze, M., Josse, F., Mrksich, M., et al. (1997). On-line detection of nonspecific protein adsorption at artificial surfaces. Analytical Chemistry, 69(16), 3321-3328. doi:10.1021/ac970047b.

Cite as: https://hdl.handle.net/21.11116/0000-0001-B4EC-A

Abstract

A detailed understanding of the interaction of proteins with artificial surfaces is essential for many applications in medicine and biochemistry. The affinity of surfaces toward proteins may, for instance, remove pharmacological proteins from media or control the adherence of pathogenic bacteria to protheses. Only a few analytical techniques now exist that can be used to study the binding process in real time, using unlabeled proteins. By investigating the adsorption kinetics of fibrinogen at differently terminated self-assembled monolayers (SAMs) of alkanethiols on thin gold films, it is demonstrated that acoustic plate-mode sensors are a promising analytical tool for studying the adsorption of proteins. In agreement with previous studies for fibrinogen, it is shown in situ that hexa(ethylene glycol)-terminated SAMs (HS(CH2)11(OCH2CH2)6OH) exhibit very low protein adsorption and that methyl-terminated SAMs (HS(CH2)11CH3) tend to adsorb large amounts of protein nonspecifically. The observed adsorption kinetics deviate from classical Langmuir behavior; these kinetics are compatible with a mechanism that involves an unfolding of fibrinogen after adsorption. Film quality is controlled by IR, XPS, and contact angle measurements.