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

Type
Label
  • Electrophysiology Investigation of Trichogin GA IV Activity in Planar Lipid Membranes Reveals Ion Channels of Well-Defined Size (Articolo in rivista) (literal)
Anno
  • 2014-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/cbdv.201300334 (literal)
Alternative label
  • Iftemi, Sorana; De Zotti, Marta; Formaggio, Fernando; Toniolo, Claudio; Stella, Lorenzo; Luchian, Tudor (2014)
    Electrophysiology Investigation of Trichogin GA IV Activity in Planar Lipid Membranes Reveals Ion Channels of Well-Defined Size
    in Chemistry & biodiversity (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Iftemi, Sorana; De Zotti, Marta; Formaggio, Fernando; Toniolo, Claudio; Stella, Lorenzo; Luchian, Tudor (literal)
Pagina inizio
  • 1069 (literal)
Pagina fine
  • 1077 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 11 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 9 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 7 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Physics, Laboratory of Molecular Biophysics and Medical Physics, Alexandru I. Cuza University, 11, Blvd. Carol I, RO-700506 Iasi; ICB, Padova Unit, CNR, Department of Chemistry, University of Padova, IT-35131 Padova; Department of Chemical Sciences and Technologies, University of Rome \"Tor Vergata\", via della Ricerca Scientifica 1, IT-00133 Rome; Department of Interdisciplinary Science, Alexandru I. Cuza University, RO-700506 Iasi (literal)
Titolo
  • Electrophysiology Investigation of Trichogin GA IV Activity in Planar Lipid Membranes Reveals Ion Channels of Well-Defined Size (literal)
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. (literal)
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