title: Nanotechnology with s-layer proteins.
abstract: Nanosciences are distinguished by the cross-fertilization of biology, chemistry, material sciences, and solid-state physics and hence open up a great variety of new opportunities for innovation. The technological utilization of self-assembly systems, wherein molecules spontaneously associate under equilibrium conditions into reproducible supramolecular aggregates, is one key challenge in nanosciences for life and nonlife science applications. The attractiveness of such processes is due to their ability to build uniform, ultrasmall functional units and the possibility to exploit such structures at meso- and macroscopic scale very frequently by newly developed techniques and methods. By the utilization of crystalline bacterial cell-surface proteins (S-layer proteins) innovative approaches for the assembly of supramolecular structures and devices with dimensions of a few to tens of nanometers have been developed. S-layers have proven to be particularly suited as building blocks in a molecular construction kit involving all major classes of biological molecules. The controlled immobilization of biomolecules in an ordered fashion on solid substrates and their controlled confinement in definite areas of nanometer dimensions are key requirements for many applications including the development of bioanalytical sensors, biochips, molecular electronics, biocompatible surfaces, and signal processing between functional membranes, cells, and integrated circuits.
authors.affiliation: Department of NanoBiotechnology, University of Natural Resources and Life Sciences, Vienna, Austria.
authors.forename: Bernhard
authors.initials: B
authors.lastname: Schuster
authors.forename: Uwe B
authors.initials: UB
authors.lastname: Sleytr
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry / Q000648:ultrastructure; D001407:Bacillus; D001426:Bacterial Proteins / Q000737:chemistry* / Q000648:ultrastructure; D006801:Humans; D055767:Immobilized Proteins / Q000737:chemistry; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000648:ultrastructure; D008567:Membranes, Artificial; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D053758:Nanoparticles / Q000737:chemistry; D036103:Nanotechnology; D011485:Protein Binding; D013499:Surface Properties; D013822:Thermoplasma
chemical_list: D019843:Archaeal Proteins; D001426:Bacterial Proteins; D055767:Immobilized Proteins; D008562:Membrane Glycoproteins; D008567:Membranes, Artificial; C055764:S-layer proteins