Self-Assembling Cages from Coiled-Coil Peptide Modules

• DOI: 10.1126/science.1233936
• Publication Date: 2013-04-12T03:50:28Z
• Authors: Jordan M. Fletcher; Robert L. Harniman; Frederick R. H. B...; Aimee L. Boyle; Andrew Collins; Judith Mantell; Thomas H. Sharp; Massimo Antognozzi; Paula J. Booth; Noah Linden; Mervyn J. Miles; Richard B. Sessions; Paul Verkade; Derek N. Woolfson
• Keywords: Models, Molecular; Protein Structure; Secondary; Protein Folding; Protein Conformation; /dk/atira/pure/core/keywords/biodesign_SRI; Molecular Dynamics Simulation; Electron; 01 natural sciences; Protein Structure, Secondary; Models; Scanning; Microscopy; Circular Dichroism; Molecular; 500; 540; Nanostructures; 0104 chemical sciences; Microscopy, Electron, Scanning; Thermodynamics; synthetic biology; name=Bristol BioDesign Institute; Protein Multimerization; Peptides

From Coils to Cages

Self-assembly strategies that mimic protein assembly, such as the formation of viral coats, often begin with simpler peptide assemblies.

Fletcher et al.

(p. 595 , published online 11 April; see the Perspective by

Ardejani and Orner

) designed two coiled-coil peptide motifs, a heterodimer, and a homotrimer. Both peptides contained cysteine residues and could link through disulfide bonds, so that the trimer could form the vertices of a hexagonal network and the dimer its edges. However, these components are flexible and, rather than form extended sheets, they closed to form particles ∼100 nanometers in diameter.