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Ion channel formation by synthetic analogues of staphylococcal δ-toxin

Abstract:

Ion channel formation by three analogues of staphylococcal δ-toxin, an amphipathic and α-helical channel-forming peptide, has been evaluated by measurement of ionic currents across planar lipid bilayers. Replacement of β-branched, hydrophobic residues by leucine and movement of a tryptophan residue from the hydrophilic to the hydrophobic face of the helix does not significantly alter ion channel activity. Removal of the N-terminal blocking group combined with the substitution of glycine-10...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/0005-2736(95)00051-4

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
Wellcome Tust More from this funder
Science and Engineering Research Council More from this funder
Publisher:
Elsevier
Journal:
Biochimica et Biophysica Acta (BBA) - Biomembranes Journal website
Volume:
1236
Issue:
2
Pages:
219–227
Publication date:
1995-06-01
DOI:
ISSN:
0005-2736
Language:
English
Subjects:
UUID:
uuid:ad934f2e-5877-46a0-bd84-97618bd12735
Local pid:
ora:8103
Deposit date:
2014-02-26

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