Patterning of Crystalline S-Layer Protein Layers

Erika S. Györvary1, Alan O'Riordan2, Aidan Quinn2, Gareth Redmond2, Dietmar Pum1, and Uwe B. Sleytr1 1Center for Ultrastructure Research, Ludwig Boltzmann Institute for Molecular Nanotechnology, University of Agricultural Sciences, Gregor-Mendel-Strasse 33, A-1180 Vienna, Austria, and 2Nanotechnology Group, National Microelectronics Research Center, Lee Maltings, Prospect Row, Cork, Ireland e-mail: gyoervar@edv1.boku.ac.at URL: http://www.boku.ac.at/zuf/nano0.htm

Self-assembly is one of the key technologies in nanosciences for building supramolecular architectures involving bottom up strategies. An unique self-assembly system was developed by nature in the form of two-dimensional protein crystals on the surface of bacterial and archaeal cell envelopes. The ability of these surface layer (S-layer) protein subunits to crystallize also on technologically important interfaces makes S-layer proteins to interesting building blocks in molecular nanobiotechnology. It is necessary to spatially control the assembly of S-layers with micron and submicron resolution on the solid substrate. For this patterning task, soft lithographical method, micromoulding in capillaries, was utilised. The obtained crystalline protein structures were characterized by fluorescence microscopy and atomic force microscopy. S-layers on silicon or gold surfaces are expected to be a key element in applications of molecular nanotechnology and highly integrated biosensors (Lab-on-Chip).