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A monodisperse transmembrane α-helical peptide barrel.

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 transport...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/nchem.2647

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
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Royal Society More from this funder
Publisher:
Nature Publishing Group Publisher's website
Journal:
Nature Chemistry Journal website
Volume:
9
Issue:
5
Pages:
411-419
Publication date:
2016-11-05
Acceptance date:
2016-09-13
DOI:
EISSN:
1755-4349
ISSN:
1755-4330
Pubs id:
pubs:690868
URN:
uri:a72471f3-0aa4-4ecd-9e3f-cddb91f35f6b
UUID:
uuid:a72471f3-0aa4-4ecd-9e3f-cddb91f35f6b
Local pid:
pubs:690868
Language:
English
Keywords:

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