Metal-induced self-assembly of peroxiredoxin as a tool for sorting ultrasmall gold nanoparticles into one-dimensional clusters

Abstract

Nanomanipulation of matter to create responsive, ordered materials still remains extremely challenging. Supramolecular chemistry has inspired new strategies by which such nanomaterials can be synthesized step by step by exploiting the self-recognition properties of molecules. In this work, the ring-shaped architecture of the 2-Cys peroxiredoxin I protein from Schistosoma mansoni, engineered to have metal ion-binding sites, is used as a template to build up 1D nanoscopic structures through metal-induced self-assembly. Chromatographic and microscopic analyses demonstrate the ability of the protein rings to stack directionally upon interaction with divalent metal ions and form well-defined nanotubes by exploiting the intrinsic recognition properties of the ring surfaces. Taking advantage of such behavior, the rings are then used to capture colloidal Ni(2+)-functionalized ultrasmall gold nanoparticles and arrange them into 1D arrays through stacking into peapod-like complexes. Finally, as the formation of such nano-peapods strictly depends on nanoparticle dimensions, the peroxiredoxin template is used as a colloidal cut-off device to sort by size the encapsulated nanoparticles. These results open up possibilities in developing Prx-based methods to synthesize new advanced functional materials.

Cryo-Electron Microscopy Structure of Human Peroxiredoxin-3 Filament Reveals the Assembly of a Putative Chaperone

“…In addition to a putative biomedical relevance, the ability of Prxs to form such organized supramolecular HMW assemblies in a switch-like fashion makes them an attractive candidate for application in protein nanotechnology (Phillips et al, 2014). For instance, Ardini et al (2014) demonstrated the use of Prx tubes as nano-peapods for ultra-small gold particles, which could be useful as nanowires.…”

Protein nanorings organized by poly(styrene-block-ethylene oxide) self-assembled thin films

“…Previous work on creating protein assemblies has been largely centered around amyloid fibers [25][26][27][28][29] but has recently also involved native protein structures [30][31][32] with ring shaped proteins emerging as a commonly used self-assembling feature. [33][34][35][36][37] Recent work has established methods to post functionalize assembled structures, 38,39 an important step towards applications based on protein nanostructures. There is intense interest in "one-dimensional nanostructures".…”

“…We seek here to harness the unique features of a protein, Lsmα from Methanobacterium thermoautotrophicum, which was selected for its thermostability and ability to self-assemble into a heptameric ring. 40,41 Proteins like Lsmα and peroxiredoxin 36 self-assemble into robust doughnuts whose pore size can be tuned specifically to encapsulate metal complexes or nanoparticles 37 and then assemble further into tunnels to create magnetic, electrical or optical nanorods. Accordingly, we have explored the possibility of using self-assembled block copolymers as scaffolds to create regular arrays of such doughnut tunnels.…”

Highly ordered protein cage assemblies: A toolkit for new materials

“…Prxs belong to an abundant family of peroxide-dependent antioxidant enzymes within cells (Perkins, Nelson, Parsonage, Poole, & Karplus, 2015;Rhee, Chae, & Kim, 2005). Although Prxs can be found as CP dimers in solution, decameric toroidal capsids with an approximate outer diameter of 13 nm, an inner pore of 6 nm, and a height of 4 nm are more commonly found (Ardini et al, 2014;Domigan et al, 2017;Jang et al, 2004) (Figure 1g). Furthermore, larger aggregates and higherorder complexes such as toroid stacks or spherical cages are naturally found under reducing conditions (Lowther & Haynes, 2011;Phillips et al, 2014).…”

“…Copyright 2018 American Chemical Society, Medalsy et al (2008). Copyright 2008 American Chemical Society, Ardini et al (2014). Copyright 2014 Royal Society of Chemistry, and Sendai et al (2013).…”