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 W; 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.

Electrophysiology Investigation of Trichogin GA IV Activity in Planar Lipid Membranes Reveals Ion Channels of Well-Defined Size

Formaggio Fernando;Toniolo Claudio;
2014

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 W; 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.
2014
Istituto di Chimica Biomolecolare - ICB - Sede Pozzuoli
Inglese
11
7
1069
1077
9
Sì, ma tipo non specificato
2
info:eu-repo/semantics/article
262
Iftemi, Sorana; De Zotti, Marta; Formaggio, Fernando; Toniolo, Claudio; Stella, Lorenzo; Luchian, Tudor
01 Contributo su Rivista::01.01 Articolo in rivista
none
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/227777
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