The interaction of cationic antimicrobial peptides with vesicles containing synthetic glycolipids as models of the outer membrane of Gram-negative bacteria (Articolo in rivista)

Type
Label
  • The interaction of cationic antimicrobial peptides with vesicles containing synthetic glycolipids as models of the outer membrane of Gram-negative bacteria (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/psc.695 (literal)
Alternative label
  • Marina Gobbo; Laura Biondi; Fernando Filira; Raniero Rocchi (2006)
    The interaction of cationic antimicrobial peptides with vesicles containing synthetic glycolipids as models of the outer membrane of Gram-negative bacteria
    in Journal of peptide science (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Marina Gobbo; Laura Biondi; Fernando Filira; Raniero Rocchi (literal)
Pagina inizio
  • 132 (literal)
Pagina fine
  • 139 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 12 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Chemical Sciences, University of Padova, Institute of Biomolecular Chemistry, CNR, I-23131 Padova, Italy (literal)
Titolo
  • The interaction of cationic antimicrobial peptides with vesicles containing synthetic glycolipids as models of the outer membrane of Gram-negative bacteria (literal)
Abstract
  • Two simple lipid A analogues methyl 2,3-di-O-tetradecanoyl-alpha-D-glucopyranoside (GL1) and methyl 2,3-di-O-tetradecanoyl-alpha-D-glucopyranoside 4-O-phosphate (GL2) were synthesized and used for preparing mixed phosphocholine vesicles as models of the outer membrane of gram-negative bacteria. The interaction of these model membranes with magainin 2, a representative of the a-helical membrane active peptides, and apidaccin Ib and drosocin, two insect Pro-rich peptides which do not act at the level of the cellular membrane, were studied by CID and dye-releasing experiments. The CD spectra of apidaecin Ib and drosocin in the presence of GL1- or GL2-containing vesicles were consistent with largely unordered structures, whereas, according to the CD spectra, magainin 2 adopted an amphipathic a-helical conformation, particularly in the presence of negatively charged bilayers. The ability of the peptides to fold into amphipathic conformations was strictly correlated to their ability to bind and to permeabilize phospholipid as well as glycolipid membranes. Apidaecin Ib and drosocin, which are unable to adopt an amphipathic structure, showed negligible dye-leakage activity even in the presence of GL2-containing vesicles. It is reasonable to suppose that, as for the killing mechanism, the two classes of antimicrobial peptides follow different patterns to cross the bacterial outer membrane. (literal)
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