Laura J. Domigan1, Kyle Webster1, Helen Ashmead2, Rishi Pande3, Jenny Malmstrom1,5, Matthew Blunt4, David E. Williams1,5, and Juliet A. Gerrard1,5*

 

1 University of Auckland, Auckland, New Zealand
2 Callaghan Innovation, Lower Hutt, New Zealand
3 University of Canterbury, Christchurch, New Zealand
4 University College London, London, UK
5 MacDiarmid Institute for Advanced Materials and Nanotechnology, Wellington, New Zealand

 

Recent research has highlighted the exciting possibility to use protein structures as a means to spatially organise more classical nanocomponents, with the goal of forming functional nanodevices [1,2]. In order to do this effectively, control over protein-protein, and protein-surface interactions is essential. In this study we are concerned with the interaction of human peroxiredoxin 3 with model surfaces, a protein that has been previously identified as having potential use in nanotechnology [3,4].

Analytical ultracentrifugation and transmission electron microscopy (TEM) revealed the pH-mediated assembly of protein toroids into tubular structures across a small, physiological pH range. Quartz crystal microbalance with dissipation (QCM-D) was used to monitor the adsorption of protein structures on surfaces, with scanning tunnelling microscopy (STM) supporting the formation of protein tubes on gold surfaces.

To form higher-order hierarchical structures, peroxiredoxin, and a peptide inspired by the dimer-dimer interface of peroxiredoxin, were assembled into peptide bound protein arrays. These were characterised by QCM-D and TEM, with gold nanoparticles incorporated as proof-of-concept towards the development of a functionalizable system.

 

References

  1. L. Miao et al. Chem. Commun., 2016, 52, 1359-7345
  2. J. Malmstrom et al. Nanoscale 2015, 47, 19940-19948
  3. M. Ardini et al. Nanoscale 2016, 8, 6739-6753
  4. A.J. Phillips et al. Biomacromolecules 2014, 15, 1871-1811

Venue

Room: 
Hawken N201