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A monodisperse transmembrane α-helical peptide barrel

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)411–419
Number of pages9
JournalNature Chemistry
Volume9
Issue number5
Early online date14 Nov 2016
DOIs
DateAccepted/In press - 13 Sep 2016
DateE-pub ahead of print - 14 Nov 2016
DatePublished (current) - May 2017

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.

    Structured keywords

  • Bristol BioDesign Institute
  • BrisSynBio

    Research areas

  • Biosensors, Membranes, synthetic biology

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  • Full-text PDF (accepted author manuscript)

    Rights statement: This is the accepted author manuscript (AAM). The final published version (version of record) is available online via Nature Publishing Group at http://doi.org/10.1038/nchem.2647. Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 1 MB, PDF document

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