Self-Assembling Cages from Coiled-Coil Peptide Modules

Author:

Fletcher Jordan M.1,Harniman Robert L.123,Barnes Frederick R. H.1,Boyle Aimee L.1,Collins Andrew14,Mantell Judith5,Sharp Thomas H.15,Antognozzi Massimo23,Booth Paula J.5,Linden Noah6,Miles Mervyn J.23,Sessions Richard B.5,Verkade Paul57,Woolfson Derek N.15

Affiliation:

1. School of Chemistry, Cantock’s Close, University of Bristol, Bristol BS8 1TS, UK.

2. School of Physics, H. H. Wills Physics Laboratory, Tyndall Avenue, University of Bristol, Bristol BS8 1TL, UK.

3. Centre for Nanoscience and Quantum Information (NSQI), Tyndall Avenue, University of Bristol, Bristol BS8 1FD, UK.

4. Bristol Centre for Functional Nanomaterials, NSQI, Tyndall Avenue, University of Bristol, Bristol BS8 1FD, UK.

5. School of Biochemistry, Medical Sciences Building, University Walk, University of Bristol, Bristol BS8 1TD, UK.

6. School of Mathematics, University Walk, University of Bristol, Bristol BS8 1TW, UK.

7. School of Physiology and Pharmacology, Medical Sciences Building, University Walk, University of Bristol, Bristol BS8 1TD, UK.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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