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) › peer-review

456 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

Research Groups and Themes

Bristol BioDesign Institute
Organic & Biological

Keywords

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

Access to Document

10.1126/science.1233936

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

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Development of supramolecular assemblies for enhancing cellular productivity and the synthesis of fine chemicals and biotheraputics.
Woolfson, D. N. (Principal Investigator), Cryan, M. J. (Principal Investigator) & Verkade, P. (Principal Investigator)
1/10/14 → 30/09/19
Project: Research, Parent
3-month Core Capability for Chemistry Research
Crosby, J. (Principal Investigator)
1/01/13 → 1/04/13
Project: Research
A BIOMOLECULAR-DESIGN APPROACH IN SYNTHETIC BIOLOGY: TOWARDS SYNTHETIC CYTOSKELETONS
Woolfson, D. N. (Principal Investigator)
1/07/09 → 1/07/13
Project: Research

HPC (High Performance Computing) and HTC (High Throughput Computing) Facilities
Alam, S. R. (Manager), Williams, D. A. G. (Manager), Eccleston, P. E. (Manager) & Greene, D. (Manager)
Facility/equipment: Facility

Cite this

@article{25c373628f064f23985a5d3197de2ed7,

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

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.\}",

year = "2013",

month = may,

day = "3",

doi = "10.1126/science.1233936",

language = "English",

volume = "340",

pages = "595--599",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

number = "6132",

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TY - JOUR

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 - synthetic biology

KW - Protein Folding

KW - Circular Dichroism

KW - Peptides

KW - Protein Conformation

KW - Nanostructures

KW - Microscopy, Electron, Scanning

KW - Models, Molecular

KW - Molecular Dynamics Simulation

KW - Thermodynamics

KW - Protein Multimerization

KW - Protein Structure, Secondary

U2 - 10.1126/science.1233936

DO - 10.1126/science.1233936

M3 - Article (Academic Journal)

C2 - 23579496

SN - 0036-8075

VL - 340

SP - 595

EP - 599

JO - Science

JF - Science

IS - 6132

ER -

Self-assembling cages from coiled-coil peptide modules

Abstract

Research Groups and Themes

Keywords

Access to Document

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Projects

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

3-month Core Capability for Chemistry Research

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

Equipment

HPC (High Performance Computing) and HTC (High Throughput Computing) Facilities

Cite this