PMID: 7540163Feb 1, 1995Paper

Conformational study of a synthetic analogue of alamethicin. Influence of the conformation on ion-channel lifetimes

International Journal of Peptide and Protein Research
L BrachaisGérard Molle

Abstract

Alamethicin, a 20-residue peptaibol, induces voltage-dependent ion channels in lipid bilayers according to the barrel-stave model. A synthetic analogue (L2) in which all Aib were replaced by Leu shows a conductance behaviour similar to alamethicin, but channel lifetimes are drastically reduced. Among several hypotheses, a different conformation for L2 might be responsible for this phenomenon by increasing the alpha-helical content (alamethicin presents some 3.0(10)-helical parts) and thus decreasing the length of the transmembrane part. A conformational study of L2 was undertaken using FTIR, CD and NMR spectroscopy, and the secondary structure was compared with alamethicin. These techniques showed an enhanced predominant helical structure as compared to alamethicin. Moreover, the NOE pattern showed an exclusively alpha-helical conformation, resulting in a smaller length of the L2 peptide. This shortening somewhat impedes the complete crossing of the membrane, and could then explain the reduction of its ion-channel lifetimes.

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Citations

Sep 30, 1998·Journal of Peptide Science : an Official Publication of the European Peptide Society·L BrachaisG Molle
Aug 26, 1998·The Journal of Peptide Research : Official Journal of the American Peptide Society·R AndersL R Brown
Jun 26, 2007·Chemistry & Biodiversity·Sonia RippaLaure Béven

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