|Dietmar Pum, Nicola Ilk, Bernd Schuster, and Uwe B. Sleytr
Center for NanoBiotechnology, University of Natural Resources and Applied Life Sciences, 1180 Vienna, Austria
One of the most challenging research areas is currently found at the interface between biology and physics. In particular, bottom fabrication and self-assembly of molecular building locks has grown into a scientific and engineering discipline crossing the boundaries of several established fields.
Two-dimensional bacterial surface layer proteins (S-layer proteins), isolated from prokaryotic organisms (bacteria and archaea), have the intrinsic tendency to self-assembly into two-dimensional arrays in suspension, at solid supports (e.g. silicon wafers), at the air-water interface, at floating lipid monolayers and at vesicles (liposomes and nanocapsules).
This presentation is focussing on the reassembly of native and genetically functionalized S-layer proteins on solid supports and, in particular, on their use as matrices for the templated assembly of molecules and nanoparticles into highly ordered superlattices. S-layer fusion proteins with different functionalities play the key role in this approach. This concept is of a more general nature and is currently used in the development of new affinity matrices, diagnostics, vaccines, biocompatible surfaces, microcarriers, and biological templating, or specific biomineralisation strategies on surfaces.