Membrane thickness and the mechanism of action of the short peptaibol trichogin GA IV (Articolo in rivista)

Type
Label
  • Membrane thickness and the mechanism of action of the short peptaibol trichogin GA IV (Articolo in rivista) (literal)
Anno
  • 2013-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bbamem.2012.11.033 (literal)
Alternative label
  • S. Bobone, Y. Gerelli, M. De Zotti, G. Bocchinfuso, A. Farrotti, B. Orioni, F. Sebastiani, E. Latter, J. Penfold, R. Senesi, F. Formaggio, A. Palleschi, C. Toniolo, G. Fragneto, L. Stella (2013)
    Membrane thickness and the mechanism of action of the short peptaibol trichogin GA IV
    in Biochimica et biophysica acta. Biomembranes
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • S. Bobone, Y. Gerelli, M. De Zotti, G. Bocchinfuso, A. Farrotti, B. Orioni, F. Sebastiani, E. Latter, J. Penfold, R. Senesi, F. Formaggio, A. Palleschi, C. Toniolo, G. Fragneto, L. Stella (literal)
Pagina inizio
  • 1013 (literal)
Pagina fine
  • 1024 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 1828 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Univ Roma Tor Vergata, Dept Chem Sci & Technol, I-00133 Rome, Italy; ILL Grenoble, F-38000 Grenoble, France; Institute of Biomolecular Chemistry, Padova Unit, CNR, Department of Chemistry, University of Padova, 35131 Padova, Italy; Rutherford Appleton Lab, ISIS, STFC, Didcot OX11 0QX, Oxon, England; Univ Roma Tor Vergata, Dept Phys and Ctr NAST, I-00133 Rome, Italy; CNR, IPCF, Italy (literal)
Titolo
  • Membrane thickness and the mechanism of action of the short peptaibol trichogin GA IV (literal)
Abstract
  • Trichogin GA IV (GAIV) is an antimicrobial peptide of the peptaibol family, like the extensively studied alamethicin (Alm). GAIV acts by perturbing membrane permeability. Previous data have shown that pore formation is related to GAIV aggregation and insertion in the hydrophobic core of the membrane. This behavior is similar to that of Alm and in agreement with a barrel-stave mechanism, in which transmembrane oriented peptides aggregate to form a channel. However, while the 19-amino acid long Alm has a length comparable to the membrane thickness, GAIV comprises only 10 amino acids, and its helix is about half the normal bilayer thickness. Here, we report the results of neutron reflectivity measurements, showing that GAIV inserts in the hydrophobic region of the membrane, causing a significant thinning of the bilayer. Molecular dynamics simulations of GAIV/membrane systems were also performed. For these studies we developed a novel approach for constructing the initial configuration, by embedding the short peptide in the hydrophobic core of the bilayer. These calculations indicated that in the transmembrane orientation GAIV interacts strongly with the polar phospholipid headgroups, drawing them towards its N- and C-termini, inducing membrane thinning and becoming able to span the bilayer. Finally, vesicle leakage experiments demonstrated that GAIV activity is significantly higher with thinner membranes, becoming similar to that of Alm when the bilayer thickness is comparable to its size. Overall, these data indicate that a barrel-stave mechanism of pore formation might be possible for GAIV and for similarly short peptaibols despite their relatively small size. (literal)
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