Self-Assembling Cages from Coiled-Coil Peptide Modules

Models, Molecular 0301 basic medicine Protein Structure Secondary Protein Folding Protein Conformation /dk/atira/pure/core/keywords/biodesign_SRI Molecular Dynamics Simulation Electron 01 natural sciences Protein Structure, Secondary 03 medical and health sciences 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
DOI: 10.1126/science.1233936 Publication Date: 2013-04-12T03:50:28Z
ABSTRACT
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.
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