Channel properties of template assembled alamethicin tetramers

The multiple conductance levels displayed by the antibiotic alamethicin in planar lipid bilayers is explained by a dynamic ‘barrel‐stave’ model, the conducting pore resulting from the aggregation of up to ten helical amphipathic helical monomers. However, the precise assignment of an oligomerization...

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Veröffentlicht in:	Journal of peptide science 2003-11, Vol.9 (11-12), p.776-783
Hauptverfasser:	Duclohier, Hervé, Alder, Glenn, Kociolek, Karol, Leplawy, Miroslaw T.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alamethicin - chemistry Amino Acid Sequence Anti-Bacterial Agents - chemistry channel forming peptides conductances Dimerization Electrophysiology Fungal Proteins - chemistry Ion Channels - chemical synthesis Ion Channels - physiology Ionophores - chemistry Lipid Bilayers Molecular Mimicry peptaibols planar lipid bilayers template assembled synthetic proteins voltage-dependence
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