Formation of supramolecular protein structures on gold surfaces

Laura Domigan, Helen Ashmead, Simone Dimartino, Jenny Malmstrom, Grant Pearce, Matthew Blunt, David Williams, Juliet Gerrard

Research output: Contribution to journalArticlepeer-review


Recent research has highlighted the exciting possibilities enabled by the use of protein structures as nanocomponents to form functional nanodevices. To this end, control over protein-protein and protein-surface interactions is essential. In this study, the authors probe the interaction of human peroxiredoxin 3 with gold surfaces, a protein that has been previously identified as having potential use in nanotechnology. Analytical ultracentrifugation and transmission electron microscopy revealed the pH mediated assembly of protein toroids into tubular structures across a small pH range. Quartz crystal microbalance with dissipation measurements showed differences in absorbed protein mass when pH is switched from pH 8.0 to 7.2, in line with the formation of supramolecular structures observed in solution studies. Scanning tunneling microscopy under ambient conditions showed that these protein tubes form on surfaces in a concentration dependent manner, with a tendency for protein adsorption and supramolecular assembly at the edges of Au(111) terraces. Finally, self-assembled monolayer modification of Au surfaces was explored as a means to control the adsorption and orientation of pH triggered protein structures.

Original languageEnglish
Pages (from-to)04E405
Issue number4
Early online date15 Nov 2017
Publication statusPublished - 15 Nov 2017


  • Gold
  • Humans
  • Hydrogen-Ion Concentration
  • Macromolecular Substances
  • Microscopy, Electron, Transmission
  • Microscopy, Scanning Tunneling
  • Nanotubes
  • Peroxiredoxin III
  • Protein Multimerization
  • Quartz Crystal Microbalance Techniques
  • Ultracentrifugation
  • Journal Article


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