A monodisperse transmembrane α-helical peptide barrel

Mahendran, K. R., Niitsu, A., Kong, L., Thomson, A. R. , Sessions, R. B., Woolfson, D. N. and Bayley, H. (2017) A monodisperse transmembrane α-helical peptide barrel. Nature Chemistry, 9(5), pp. 411-419. (doi:10.1038/NCHEM.2647) (PMID:28430192)

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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.

Item Type:Articles
Additional Information:The authors acknowledge a Biotechnology and Biological Sciences Research Council grant (BB/J009784/1) and the European Research Council (340764) for financial support.
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Thomson, Dr Drew
Authors: Mahendran, K. R., Niitsu, A., Kong, L., Thomson, A. R., Sessions, R. B., Woolfson, D. N., and Bayley, H.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Nature Chemistry
Publisher:Nature Publishing Group
ISSN:1755-4330
ISSN (Online):1755-4349
Published Online:14 November 2016
Copyright Holders:Copyright © 2017 Macmillan Publishers Limited, part of Springer Nature
First Published:First published in Nature Chemistry 9(5): 411-419
Publisher Policy:Reproduced in accordance with the publisher copyright policy

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