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O: Fachverband Oberflächenphysik

O 41: Inorganic/Organic Interfaces

O 41.5: Poster

Dienstag, 17. März 2015, 18:15–21:00, Poster B

Templated Protein Adsorption on Cu₂N — •Sebastian Koslowski¹, Daniel P. Rosenblatt¹, Sabine Abb¹, Stephan Rauschenbach¹, Klaus Kern^1,2, and Uta Schlickum¹ — ¹Max-Planck-Institut für Festkörperforschung, Heisenbergstrasse 1, D-70569 Stuttgart,Germany — ²Institut de Physique de la Matière Condensée, Ecole Polytechnique Fédérale de Lausanne (EPFL),CH-1015 Lausanne, Switzerland

In recent investigations of the protein Cytochrome-C (CytC) deposited on metallic substrates by electrospray ion beam deposition (ES-IBD) it has been shown that the adsorption conformation of the unfolded protein is strongly influenced by surface mobility and the charge state of the gas phase protein ion [1]. The length and the flexibility of the peptide chain allows for a large conformational freedom in the gas phase as well as on homogenous surfaces. Here we present scanning tunneling microscopy (STM) investigations of the conformation of single CytC molecules deposited by ES-IBD on a Cu₂N monolayer. Cu₂N forms an adlayer with a square grid-like superstructure on the underlying Cu(100) substrate and acts as a template for the deposited proteins. This reduces their conformational freedom. We analyzed the surface conformations of CytC using models, which describe polymer adhesion on a grid with and without the assumption of memory of the gas phase conformation. The acquired data are best described by a model, in which elongated molecules try to reach the pure Cu rows with minimal movement.
Z. Deng et al., Nano Lett. 12 (2012) 2452-2458