Poster Presentation 12th Australian Peptide Conference 2017

Parallel and antiparallel cyclic D/L peptide nanotubes (#126)

Mitchell R Silk 1 , Janet Newman 2 , Julian C Ratcliffe 3 , Jacinta F White 3 , Tom Caradoc-Davies 4 , Jason R Price 4 , Sebastien Perrier 5 , Philip E Thompson 1 , David K Chalmers 1
  1. Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Melbourne, VICTORIA, Australia
  2. Biomedical Program, CSIRO, Parkville, Victoria, Australia
  3. CSIRO manufacturing, CSIRO, Clayton, Victoria, Australia
  4. Australian Synchrotron, Clayton, Victoria, Australia
  5. Department of Chemistry, University of Warwick , Coventry, United Kingdom

Self-assembling nanotubes made from H-bonded cyclic D/L peptide (CP) subunits have great potential for the construction of nanomaterials of vast chemical and structural diversity. They have potential applications as drug-delivery vehicles, synthetic membranes and protein/ion-channels but difficulties in structure-characterisation and poor control over nanotube assembly hinder their development into functional nanomaterials. We present the first crystal structures of continuous CP nanotubes with antiparallel and parallel stacking arrangements, assembled separately from two peptides; cyclo[(Asp-D-Leu-Lys-D-Leu)2] and cyclo[(Asp-D-Ala-Lys-D-Ala)2]. Along with X-ray crystallographic studies, the peptide structures were analysed by in-solution and solid-state techniques including DLS, cryo-TEM and FT-IR. Together, these studies provide insight towards the intermolecular interactions between cyclic peptide subunits that will be critical in directing and controlling the self-assembly process to develop complex organic, functionalised materials for application in biomedicine.

  1. Ghadiri et al., Nature, 1993, 366, 324-327
  2. Silk et al., Chem Commun., 2017, 53, 6613-6616