Electrophysiology Investigation of Trichogin GA IV Activity in Planar Lipid Membranes Reveals Ion Channels of Well‐Defined Size |
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| Authors: | Sorana Iftemi Marta De Zotti Fernando Formaggio Claudio Toniolo Lorenzo Stella Tudor Luchian |
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| Affiliation: | 1. Department of Physics, Laboratory of Molecular Biophysics and Medical Physics, Alexandru I. Cuza University, 11, Blvd. Carol I, RO‐700506 Iasi (phone: +40‐232‐201191);2. ICB, Padova Unit, CNR, Department of Chemistry, University of Padova, IT‐35131 Padova;3. Department of Chemical Sciences and Technologies, University of Rome ‘Tor Vergata', via della Ricerca Scientifica 1, IT‐00133 Rome (phone: +39‐06‐7259‐4463);4. Department of Interdisciplinary Science, Alexandru I. Cuza University, RO‐700506 Iasi |
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| Abstract: | Trichogin GA IV, an antimicrobial peptaibol, exerts its function by augmenting membrane permeability, but the molecular aspects of its pore‐forming mechanism are still debated. Several lines of evidence indicate a ‘barrel‐stave’ channel structure, similar to that of alamethicin, but the length of a trichogin helix is too short to span a normal bilayer. Herein, we present electrophysiology measurements in planar bilayers, showing that trichogin does form channels of a well‐defined size (R=4.2?109 Ω; corresponding at least to a trimeric aggregate) that span the membrane and allow ion diffusion, but do not exhibit voltage‐dependent rectification, unlike those of alamethicin. |
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| Keywords: | Peptaibols Peptides Antimicrobial peptides Trichogin GA IV Electrophysiology Lipid membranes |
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