| AVS 54th International Symposium | |
| Biomaterial Interfaces | Wednesday Sessions |
| Session BI-WeM |
| Session: | Nano-Engineered Biointerfaces |
| Presenter: | A. Turchanin, University of Bielefeld, Germany |
| Authors: | A. Turchanin, University of Bielefeld, Germany M. El-Desawy, University of Bielefeld, Germany M. Schnietz, University of Bielefeld, Germany A. Gölzhäuser, University of Bielefeld, Germany A. Tinazli, Johann Wolfgang Goethe-University, Germany H. Großmann, Johann Wolfgang Goethe-University, Germany R. Tampé, Johann Wolfgang Goethe-University, Germany H.H. Solak, Paul Scherrer Institut, Switzerland |
| Correspondent: | Click to Email |
To study protein function and interaction, there is a high demand for specific, stable, highly parallel, and functional protein arrays on solid substrates. To implement this, we propose a protein chip approach based on the combination of electron induced chemical lithography1 with aromatic self-assembled monolayers (SAMs) and multivalent chelators2 for high-affinity capturing of His-tagged proteins. Templates for functional and switchable His-tagged protein architectures were created by electron induced changes in 4’-nitro-1,1’-biphenyl-4-thiol SAMs on gold (NBPT). Chemical nanopatterns were generated in SAMs by both electron beam lithography (EBL) and extreme UV interference lithography (EUV-IL). As a model system carboxy derivative tris-NTA chelators were studied. Different steps of the protein chip assembly (fabrication of amino terminated cross-linked areas, generation of protein repellent EG3-OH thiols matrix, grafting of tris-NTA chelators, and chelating efficiency of Ni(II) ions) were characterized in detail by X-ray photoelectron spectroscopy (XPS) and atomic force microscopy (AFM). The functionality of the generated protein chips was shown in situ, under physiological conditions by AFM and scanning fluorescence microscopy measurements via specific, homogeneous, oriented and reversible immobilization of His6-tagged 20S proteasome and fluorescence labelled His10-tagged maltose binding proteins (MBP). We will present highly parallel large area (~10 mm2) protein arrays with the lateral dimensions of periodic features ranging from 1000 nm to 50 nm.
1A. Gölzhäuser, W. Eck, W. Geyer, V. Stadler, T.Weimann, P. Hinze, M. Grunze, Adv. Mat. 13 (2001) 806
2A. Tinazli, J. Tang, R.Valiokas, S. Picuric, S. Lata, J. Piehler, B. Liedberg, R. Tampé, Chemistry 11 (2005) 5249.