Assembly of protein stacks with in situ synthesized nanoparticle cargo

Sesha Manuguri, Kyle Webster, N. Amy Yewdall, Yiran An, Hari Venugopal, Vaibhav Bhugra, Adrian Turner, Laura J. Domigan, Juliet A. Gerrard, David E. Williams, Jenny Malmström

Research output: Contribution to journalArticleAcademicpeer-review

20 Citations (Scopus)


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 Fe2+ 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.

Original languageEnglish
Pages (from-to)5138-5145
Number of pages8
JournalNano Letters
Issue number8
Publication statusPublished - 8 Aug 2018
Externally publishedYes


  • electrostatic force microscopy
  • iron-oxide mineralization
  • nanoparticle organization
  • peroxiredoxin
  • Protein nanotechnology


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