Self-assembling cages from coiled-coil peptide modules.

Journal article

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.

Authors: Fletcher, J; Harniman, R; Barnes, F; Boyle, A; Collins, A

• Journal: Science (New York, N.Y.)
• Volume: 340
• Issue: 6132
• Pages: 595-599
• Publication date: 2013-05-01
• DOI: 10.1126/science.1233936
• EISSN: 1095-9203
• ISSN: 0036-8075
• Language: English
• Keywords: Protein Folding; Models, Molecular; Protein Structure, Secondary; Peptides; Circular Dichroism; Protein Conformation; Microscopy, Electron, Scanning; Protein Multimerization; Nanostructures; Thermodynamics; Molecular Dynamics Simulation