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BP: Fachverband Biologische Physik

BP 28: Protein structure and dynamics II

BP 28.9: Vortrag

Mittwoch, 2. April 2014, 17:30–17:45, HÜL 386

Characterizing Protein Adsorption by In situ Atomic Force Microscopy at Single Protein Resolution — •Christian Kreis, Jonas Heppe, Christian Spengler, Hendrik Hähl, and Karin Jacobs — Department of Experimental Physics, Saarland University, Saarbrücken, 66041, Germany

The adsorption of proteins to surfaces is governed by the mutual interactions of proteins, solution and substrate. To fully characterize the interactions, we have shown before that also the long range van der Waals forces arising from the subsurface of the substrate have to be taken into account [1,2]. However, the uppermost layer defines the surface chemistry and is dominating the strength of the interfacial energy. Studies using e. g. ellipsometry or X-ray reflectometry observe a strong influence of the surface chemistry on protein adsorption. These studies, however, average over hundred thousands of proteins in the measurement and the spatial arrangements of the proteins remain unknown. To resolve the latter, we applied in situ AFM measurements in buffer solution and characterized the different protein distributions on hydrophilic and hydrophobic silicon wafers. Additionally, a strong denaturation of the studied proteins can be observed. These results demonstrate the influence of the surface chemistry on protein adsorption and help to elucidate the differences in adsorption kinetics or the final adsorbed layer.

[1] Y. Schmitt et al. Biomicrofluidics 4 (2010) 032201
[2] H. Hähl et al. Langmuir 28 (2012) 7747–7756