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Negatively charged flat gold nanotriangles, formed in a vesicular template phase and separated by an AOT-micelle-based depletion flocculation, were reloaded by adding a cationic polyelectrolyte, that is, a hyperbranched polyethylenimine (PEI). Heating the system to 100 degrees C in the presence of a gold chloride solution, the reduction process leads to the formation of gold nanoparticles inside the polymer shell surrounding the nanoplatelets. The gold nanoparticle formation is investigated by UV-vis spectroscopy, small-angle X-ray scattering, and dynamic light scattering measurements in combination with transmission electron microscopy. Spontaneously formed gold clusters in the hyperbranched PEI shell with an absorption maximum at 350 nm grow on the surface of the nanotriangles as hemispherical particles with diameters of similar to 6 nm. High-resolution micrographs show that the hemispherical gold particles are crystallized onto the {111} facets on the bottom and top of the platelet as well as on the edges without a grain boundary. Undulated gold nanoplatelet superstructures with special properties become available, which show a significantly modified performance in SERS-detected photocatalysis regarding both reactivity and enhancement factor.
Unique properties of eukaryote-type actin and profilin horizontally transferred to cyanobacteria
(2012)
A eukaryote-type actin and its binding protein profilin encoded on a genomic island in the cyanobacterium Microcystis aeruginosa PCC 7806 co-localize to form a hollow, spherical enclosure occupying a considerable intracellular space as shown by in vivo fluorescence microscopy. Biochemical and biophysical characterization reveals key differences between these proteins and their eukaryotic homologs. Small-angle X-ray scattering shows that the actin assembles into elongated, filamentous polymers which can be visualized microscopically with fluorescent phalloidin. Whereas rabbit actin forms thin cylindrical filaments about 100 mu m in length, cyanobacterial actin polymers resemble a ribbon, arrest polymerization at 510 lam and tend to form irregular multi-strand assemblies. While eukaryotic profilin is a specific actin monomer binding protein, cyanobacterial profilin shows the unprecedented property of decorating actin filaments. Electron micrographs show that cyanobacterial profilin stimulates actin filament bundling and stabilizes their lateral alignment into heteropolymeric sheets from which the observed hollow enclosure may be formed. We hypothesize that adaptation to the confined space of a bacterial cell devoid of binding proteins usually regulating actin polymerization in eukaryotes has driven the co-evolution of cyanobacterial actin and profilin, giving rise to an intracellular entity.