1 research outputs found
Assembly of Protein Stacks With in Situ Synthesized Nanoparticle Cargo
The
ability of proteins to form hierarchical structures through
self-assembly provides an opportunity to synthesize and organize nanoparticles.
Ordered nanoparticle assemblies are a subject of widespread interest
due to the potential to harness their emergent functions. In this
work, the toroidal-shaped form of the protein peroxiredoxin, which
has a pore size of 7 nm, was used to organize iron oxyhydroxide nanoparticles.
Iron in the form of Fe<sup>2+</sup> was sequestered into the central
cavity of the toroid ring using metal-binding sites engineered there
and then hydrolyzed to form iron oxyhydroxide particles bound into
the protein pore. By precise manipulation of the pH, the mineralized
toroids were organized into stacks confining one-dimensional nanoparticle
assemblies. We report the formation and the procedures leading to
the formation of such nanostructures and their characterization by
chromatography and microscopy. Electrostatic force microscopy clearly
revealed the formation of iron-containing nanorods as a result of
the self-assembly of the iron-loaded protein. This research bodes
well for the use of peroxiredoxin as a template with which to form
nanowires and structures for electronic and magnetic applications