Surface functionalization for technical applications using bacterial S-layers


Surface functionalization for technical applications using bacterial S-layers

Pollmann, K.; Günther, T.; Suhr, M.; Weinert, U.; Kutschke, S.; Lehmann, F.; Raff, J.

Self-assembling biomolecules are very attractive for the development of applications that are based on self-organising nanostructures. Especially the use of highly ordered proteins is an attractive approach and offer new possibilities to functionalize surfaces. In our group we use the proteinaceous paracrystalline bacterial surface layers (S-layers) that envelop bacterial cells as nanostructures for the design of materials with novel properties. These proteins are mostly composed of protein monomers with the ability to self-assemble into two-dimensional arrays on interfaces and surfaces. These features are used for the nano-patterning of various technical surfaces. The regular distributed pores of these paracrystalline arrays are binding sites for various metals and offer ideal structures for the formation of regular distributed metallic nanoclusters of a defined size [1, 2]. In addition, the proteins can be regularly modified with organic groups, thus adding additional defined functions to the nanocoatings.
Here we present our work on the functionalization of various technical surfaces using different natural bacterial S-layers. Currently we develop different applications that are based on these coatings. Examples are biosorptive materials that are of interest for a broad range of industrial applications such as bioremediation and metal recovery. Other applications include sensory layers that are based on an assembly of S-layers, aptamers and fluorophores, and catalytic surfaces that use immobilized inorganic nanoparticles as catalytic compound.
[1] Wahl, R. et al. (2001). Adv. Materials 13, 736-740
[2] Pollmann, K. et al. (2006). Biotechnol. Adv. 24, 58-68

  • Lecture (Conference)
    EURO BioMAT 2013 - European Symposium on Biomaterials and Related Areas, 23.-24.04.2013, Weimar, Deutschland

Permalink: https://www.hzdr.de/publications/Publ-18262
Publ.-Id: 18262