Journal article
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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Authors
Funding
Royal Society
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Bibliographic Details
- Publisher:
- Nature Publishing Group Publisher's website
- Journal:
- Nature Chemistry Journal website
- Volume:
- 9
- Issue:
- 5
- Pages:
- 411-419
- Publication date:
- 2016-11-01
- Acceptance date:
- 2016-09-13
- DOI:
- EISSN:
-
1755-4349
- ISSN:
-
1755-4330
- Pmid:
-
28430192
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:690868
- UUID:
-
uuid:a72471f3-0aa4-4ecd-9e3f-cddb91f35f6b
- Local pid:
- pubs:690868
- Source identifiers:
-
690868
- Deposit date:
- 2017-11-02
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- Copyright date:
- 2016
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