Projects per year
Abstract
The fabrication of monodisperse transmembrane barrels formed from short synthetic peptides has not been demonstrated previously. This is in part because of the complexity of the interactions between peptides and lipids within the hydrophobic environment of a membrane. Here we report the formation of a transmembrane pore through the self-assembly of 35 amino acid α-helical peptides. The design of the peptides is based on the C-terminal D4 domain of the Escherichia coli polysaccharide transporter Wza. By using single-channel current recording, we define discrete assembly intermediates and show that the pore is most probably a helix barrel that contains eight D4 peptides arranged in parallel. We also show that the peptide pore is functional and capable of conducting ions and binding blockers. Such α-helix barrels engineered from peptides could find applications in nanopore technologies such as single-molecule sensing and nucleic-acid sequencing.
Original language | English |
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Pages (from-to) | 411–419 |
Number of pages | 9 |
Journal | Nature Chemistry |
Volume | 9 |
Issue number | 5 |
Early online date | 14 Nov 2016 |
DOIs | |
Publication status | Published - May 2017 |
Structured keywords
- Bristol BioDesign Institute
- BrisSynBio
Keywords
- Biosensors
- Membranes
- synthetic biology
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Projects
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CCP-BioSim: Biomolecular Simulation at the Life Sciences Interface
1/07/15 → 30/04/21
Project: Research
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Equipment
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HPC (High Performance Computing) facility
Caroline E Gardiner (Manager)
IT ServicesFacility/equipment: Facility
Profiles
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Professor Dek N Woolfson
- The Bristol Centre for Nanoscience and Quantum Information
- Synthesis
- School of Chemistry - Professor of Chemistry and Biochemistry
- Soft Matter, Colloids and Materials
- Catalysis
- Biological and Archaeological Chemistry
Person: Academic (former), Academic , Member