A monodisperse transmembrane α-helical peptide barrel

Kozhinjampara R Mahendran, Ai Niitsu, L Kong, Drew Thomson, Richard Sessions, Dek Woolfson*, Hagan Bayley

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

40 Citations (Scopus)
364 Downloads (Pure)

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 languageEnglish
Pages (from-to)411–419
Number of pages9
JournalNature Chemistry
Volume9
Issue number5
Early online date14 Nov 2016
DOIs
Publication statusPublished - May 2017

Structured keywords

  • Bristol BioDesign Institute
  • BrisSynBio

Keywords

  • Biosensors
  • Membranes
  • synthetic biology

Fingerprint Dive into the research topics of 'A monodisperse transmembrane α-helical peptide barrel'. Together they form a unique fingerprint.

Cite this