Publikation

Fabrication of Highly Ordered Gold Nanoparticle Arrays Templated by Crystalline Lattices of Bacterial S-Layer Protein

Outline:

J. Tang, H. Badelt-Lichtblau, A. Ebner, J. Preiner, B. Kraxberger, H. Gruber, U. Sleytr, N. Gelbmann, P. Hinterdorfer - Fabrication of Highly Ordered Gold Nanoparticle Arrays Templated by Crystalline Lattices of Bacterial S-Layer Protein - ChemPhysChem (Online: http://onlinelibrary.wiley.com/doi/10.1002/cphc.200800507/full), 2008

Abstract:

Biomolecular self-assembly is emerging as a powerful tool for bottom-up approaches to the fabrication of functional nanoscale structures. Nanofabrication techniques based on protein[1] and DNA[2] self-assembly have been applied for nanoscale engineering of nanoparticle (NP) arrays. Bacterial cell surface layer (S-layer) proteins spontaneously self-assemble on various types of supports by forming two-dimensional crystals exhibiting different lattice symmetries (oblique, square or hexagonal) with lattice constants in the range from 3 to 30 nm.[3, 4] These excellent building blocks are usually composed of a single protein or glycoprotein species. Taking advantage of their spatially defined physical and chemical surface properties, S-layers offer an attractive approach for the fabrication of nanoparticle templates, and have been used successfully as biotemplates for the in situ nucleation of inorganic particles[1, 5] and for binding of gold NPs via electrostatic interaction.[6, 7] The possibility of genetically modifying S-layer proteins with different functional sequences[3, 4] pave the way for building a broad range of functional nanostructures through site-directed or covalent binding of molecules to S-layer templates. Herein, highly ordered arrays of 5 nm gold NPs were generated by using the repetitive pattern of a mutated S-layer protein as a binding template for well-organized arrangements.