Self-assembly of toroidal proteins explored using native mass spectrometry

N. Amy Yewdall, Timothy M. Allison, F. Grant Pearce, Carol V. Robinson, Juliet A. Gerrard

Research output: Contribution to journalArticleAcademicpeer-review

21 Citations (Scopus)
39 Downloads (Pure)


The peroxiredoxins are a well characterised family of toroidal proteins which can self-assemble into a striking array of quaternary structures, including protein nanotubes, making them attractive as building blocks for nanotechnology. Tools to characterise these assemblies are currently scarce. Here, assemblies of peroxiredoxin proteins were examined using native mass spectrometry and complementary solution techniques. We demonstrated unequivocally that tube formation is fully reversible, a useful feature in a molecular switch. Simple assembly of individual toroids was shown to be tunable by pH and the presence of a histidine tag. Collision induced dissociation experiments on peroxiredoxin rings revealed a highly unusual symmetrical disassembly pathway, consistent with the structure disassembling as a hexamer of dimers. This study provides the foundation for the rational design and precise characterisation of peroxiredoxin protein structures where self-assembly can be harnessed as a key feature for applications in nanotechnology.

Original languageEnglish
Pages (from-to)6099-6106
Number of pages8
JournalChemical Science
Issue number28
Publication statusPublished - 28 Jul 2018
Externally publishedYes


Dive into the research topics of 'Self-assembly of toroidal proteins explored using native mass spectrometry'. Together they form a unique fingerprint.

Cite this