Assembly of Protein Stacks With in Situ Synthesized Nanoparticle Cargo

Abstract

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 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.

Bio‐Assisted Tailored Synthesis of Plasmonic Silver Nanorings and Site‐Selective Deposition on Graphene Arrays

“…Unfortunately, TEM‐based procedures for nanopore fabrication are expensive and time consuming. On the contrary, alternative approaches driven by the plasmonic nanostructure can be applied to our device. In fact, a plasmonic nanostructure on an atomic thin layer of graphene has been demonstrated to enable the self‐aligned creating of pores …”

“…Note that in many proteins the carboxyl and amine‐terminal residues lie along the surface of rim and cavity thus providing two very independent surfaces for biofunctionalization . Moreover, protein data banks provide a large variety of shapes, size, surfaces, and chemical properties, which can be used to achieve nanostructures with the desired morphology and features …”

“…[42] Moreover, protein data banks provide a large variety of shapes, [43] size, [26] surfaces, [44] and chemical properties, which can be used to achieve nanostructures with the desired morphology and features. [45] In this context, ring-like proteins are likely to play a key role as they possess unique features, i.e., natural high abundance and remarkable structural stability. [46,47] In particular, 2-Cys peroxiredoxin (PRX) family members, such as the peroxiredoxin I from the human parasite Schistosoma mansoni (PRX), are particular intriguing.…”

Switching between Stacked Toroids and Helical Supramolecular Polymers in Aqueous Nanotubules

“…Tubular structures are ubiquitous in many biological systems such as protein folding and stacked toroids. [ 1–5 ] Inspired by biological tubules, a great deal of effort has been devoted to design synthetic molecules that are able to self‐assemble into folded helical tubules [ 6,7 ] and nanotubules with stacked toroids, [ 8–11 ] which is analogous to the protein tubules in nature. The tubules based on helical folding can be constructed by supramolecular approaches.…”

Highly ordered protein cage assemblies: A toolkit for new materials

“…The natural trend of Prdxs to aggregate into columnar stacks has been exploited by Gerrard's group (Domigan et al, 2017;Phillips et al, 2014;Yewdall et al, 2016), allowing the formation of rod-like iron oxyhydroxide via mineralization of the inner pore with iron citrate, followed by assembly in a mildly acidic pH. This biomimetic approach enables the synthesis of iron-containing particles restricted in size by the protein template (Manuguri et al, 2018).…”