Self-assembling cages from coiled-coil peptide modules

Jordan M. Fletcher, Robert L. Harniman, Frederick R. H. Barnes, Aimee L. Boyle, Andrew M Collins, Judith Mantell, Thomas H. Sharp, Massimo Antognozzi, Paula J. Booth, Noah Linden, Mervyn J. Miles, Richard B. Sessions, Paul Verkade, Derek N. Woolfson*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

415 Citations (Scopus)


An ability to mimic the boundaries of biological compartments would improve our understanding of self-assembly and provide routes to new materials for the delivery of drugs and biologicals and the development of protocells. We show that short designed peptides can be combined to form unilamellar spheres approximately 100 nanometers in diameter. The design comprises two, noncovalent, heterodimeric and homotrimeric coiled-coil bundles. These are joined back to back to render two complementary hubs, which when mixed form hexagonal networks that close to form cages. This design strategy offers control over chemistry, self-assembly, reversibility, and size of such particles.
Original languageEnglish
Pages (from-to)595-599
Number of pages5
Issue number6132
Publication statusPublished - 3 May 2013

Structured keywords

  • Bristol BioDesign Institute


  • Protein Structure, Secondary
  • Thermodynamics
  • Models, Molecular
  • Protein Folding
  • Circular Dichroism
  • Peptides
  • Molecular Dynamics Simulation
  • Protein Multimerization
  • Protein Conformation
  • Nanostructures
  • Microscopy, Electron, Scanning
  • synthetic biology


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