| Title | Peroxiredoxin is a versatile self-assembling tecton for protein nanotechnology |
| Publication Type | Journal Article |
| Year of Publication | 2014 |
| Authors | Phillips, A.J., Littlejohn J., Yewdall N.A., Zhu T., Valéry C., Pearce F.G., Mitra A.K., Radjainia M., and Gerrard J.A. |
| Journal | Biomacromolecules |
| Volume | 15 |
| Issue | 5 |
| Pagination | 1871 - 1881 |
| Date Published | 2014 |
| ISSN | 15257797 (ISSN) |
| Keywords | Ammonium Sulfate, article, Biophysics, carboxy terminal sequence, chemical structure, chemistry, conformational transition, Controlled assembly, crystal structure, Environmental triggers, human, Humans, Hydrogen-Ion Concentration, ionic strength, metabolism, Models, Molecular, Molecular weight, nanocage, nanomaterial, Nanotechnology, nanotube, Nanotubes, nucleotide sequence, oxidation reduction reaction, Oxidation-Reduction, particle size, peroxiredoxin 3, Peroxiredoxin III, Peroxiredoxins, pH, PRDX3 protein, human, priority journal, protein assembly, Protein Conformation, Protein family, protein structure, Proteins, Self-assembling, Single-particle analysis, static electricity, Supramolecular assemblies, Transmission electron microscopy, ultrastructure, X ray crystallography |
| Abstract | The potential for protein tectons to be used in nanotechnology is increasingly recognized, but the repertoire of stable proteins that assemble into defined shapes in response to an environmental trigger is limited. Peroxiredoxins (Prxs) are a protein family that shows an amazing array of supramolecular assemblies, making them attractive tectons. Human Prx3 (hPrx3) forms toroidal oligomers characteristic of the Prx family, but no structure has been solved to date. Here we report the first 3-D structure of this protein, derived from single-particle analysis of TEM images, establishing a dodecameric structure. This result was supported by SAXS measurements. We also present the first detailed structure of a double toroidal Prx from a higher organism determined by SPA. Guided by these structures, variants of the protein were designed to facilitate controlled assembly of protein nanostructures through the association of the toroids. We observed an enhanced population of stacked toroids, as seen by TEM; nanocages and interlocked toroids were also visible. Low pH was successfully predicted to generate long ordered nanotubes. Control over the length of the tubes was gained by adding ammonium sulfate to the assembly buffer. These versatile assembly properties demonstrate the considerable potential of hPrx3 as a tecton for protein nanotechnology. © 2014 American Chemical Society. |
| URL | http://www.scopus.com/inward/record.url?eid=2-s2.0-84900418587&partnerID=40&md5=f6ceed87b5fda740aa9f31510bfd61d3 |
| DOI | 10.1021/bm500261u |
