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
AUTHORS (14)
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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