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Self-assembling cages from coiled-coil peptide modules

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)595-599
Number of pages5
Issue number6132
DatePublished - 3 May 2013


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.

    Structured keywords

  • Bristol BioDesign Institute

    Research areas

  • 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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