Self-assembling cages from coiled-coil peptide modules

Jordan M. Fletcher; Robert L. Harniman; Frederick R. H. Barnes; Aimee L. Boyle; Andrew M Collins; Judith Mantell; Thomas H. Sharp; Massimo Antognozzi; Paula J. Booth; Noah Linden; Mervyn J. Miles; Richard B. Sessions; Paul Verkade; Derek N. Woolfson

doi:10.1126/science.1233936

Self-assembling cages from coiled-coil peptide modules

Jordan M. Fletcher, Robert L. Harniman, Frederick R. H. Barnes, Aimee L. Boyle, Andrew M Collins, Judith Mantell, Thomas H. Sharp, Massimo Antognozzi, Paula J. Booth, Noah Linden, Mervyn J. Miles, Richard B. Sessions, Paul Verkade, Derek N. Woolfson^*

^*Corresponding author for this work

Research output: Contribution to journal › Article (Academic Journal)

314 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	595-599
Number of pages	5
Journal	Science
Volume	340
Issue number	6132
DOIs	https://doi.org/10.1126/science.1233936
Publication status	Published - 3 May 2013

Structured keywords

Bristol BioDesign Institute

Keywords

Protein Structure, Secondary
Thermodynamics
Models, Molecular
Protein Folding
Circular Dichroism
Peptides
Molecular Dynamics Simulation
Protein Multimerization
Protein Conformation
Nanostructures
Microscopy, Electron, Scanning
synthetic biology

Access to Document

10.1126/science.1233936

http://www.sciencemag.org/content/340/6132/595

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Projects

4 Finished

Development of supramolecular assemblies for enhancing cellular productivity and the synthesis of fine chemicals and biotheraputics.

Woolfson, D. N., Cryan, M. J. & Verkade, P.

1/10/14 → 30/09/19

Project: Research, Parent

3-month Core Capability for Chemistry Research

Crosby, J.

1/01/13 → 1/04/13

Project: Research

A BIOMOLECULAR-DESIGN APPROACH IN SYNTHETIC BIOLOGY: TOWARDS SYNTHETIC CYTOSKELETONS

Woolfson, D. N.

1/07/09 → 1/07/13

Project: Research

Cite this

Fletcher, J. M., Harniman, R. L., Barnes, F. R. H., Boyle, A. L., Collins, A. M., Mantell, J., Sharp, T. H., Antognozzi, M., Booth, P. J., Linden, N., Miles, M. J., Sessions, R. B., Verkade, P., & Woolfson, D. N. (2013). Self-assembling cages from coiled-coil peptide modules. Science, 340(6132), 595-599. https://doi.org/10.1126/science.1233936

Fletcher, Jordan M. ; Harniman, Robert L. ; Barnes, Frederick R. H. ; Boyle, Aimee L. ; Collins, Andrew M ; Mantell, Judith ; Sharp, Thomas H. ; Antognozzi, Massimo ; Booth, Paula J. ; Linden, Noah ; Miles, Mervyn J. ; Sessions, Richard B. ; Verkade, Paul ; Woolfson, Derek N. / Self-assembling cages from coiled-coil peptide modules. In: Science. 2013 ; Vol. 340, No. 6132. pp. 595-599.

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title = "Self-assembling cages from coiled-coil peptide modules",

abstract = "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.",

keywords = "Protein Structure, Secondary, Thermodynamics, Models, Molecular, Protein Folding, Circular Dichroism, Peptides, Molecular Dynamics Simulation, Protein Multimerization, Protein Conformation, Nanostructures, Microscopy, Electron, Scanning, synthetic biology",

author = "Fletcher, {Jordan M.} and Harniman, {Robert L.} and Barnes, {Frederick R. H.} and Boyle, {Aimee L.} and Collins, {Andrew M} and Judith Mantell and Sharp, {Thomas H.} and Massimo Antognozzi and Booth, {Paula J.} and Noah Linden and Miles, {Mervyn J.} and Sessions, {Richard B.} and Paul Verkade and Woolfson, {Derek N.}",

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doi = "10.1126/science.1233936",

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Self-assembling cages from coiled-coil peptide modules. / Fletcher, Jordan M.; Harniman, Robert L.; Barnes, Frederick R. H.; Boyle, Aimee L.; Collins, Andrew M ; Mantell, Judith; Sharp, Thomas H.; Antognozzi, Massimo; Booth, Paula J.; Linden, Noah; Miles, Mervyn J.; Sessions, Richard B.; Verkade, Paul ; Woolfson, Derek N.

In: Science, Vol. 340, No. 6132, 03.05.2013, p. 595-599.

Research output: Contribution to journal › Article (Academic Journal)

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T1 - Self-assembling cages from coiled-coil peptide modules

AU - Fletcher, Jordan M.

AU - Harniman, Robert L.

AU - Barnes, Frederick R. H.

AU - Boyle, Aimee L.

AU - Collins, Andrew M

AU - Mantell, Judith

AU - Sharp, Thomas H.

AU - Antognozzi, Massimo

AU - Booth, Paula J.

AU - Linden, Noah

AU - Miles, Mervyn J.

AU - Sessions, Richard B.

AU - Verkade, Paul

AU - Woolfson, Derek N.

PY - 2013/5/3

Y1 - 2013/5/3

N2 - 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.

AB - 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.

KW - Protein Structure, Secondary

KW - Thermodynamics

KW - Models, Molecular

KW - Protein Folding

KW - Circular Dichroism

KW - Peptides

KW - Molecular Dynamics Simulation

KW - Protein Multimerization

KW - Protein Conformation

KW - Nanostructures

KW - Microscopy, Electron, Scanning

KW - synthetic biology

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DO - 10.1126/science.1233936

M3 - Article (Academic Journal)

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JO - Science

JF - Science

SN - 0036-8075

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