Aggregation and Water-Membrane Partition as Major Determinants of the Activity of the Antibiotic Peptide Trichogin GA IV. (Articolo in rivista)

Type
Label
  • Aggregation and Water-Membrane Partition as Major Determinants of the Activity of the Antibiotic Peptide Trichogin GA IV. (Articolo in rivista) (literal)
Anno
  • 2004-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/S0006-3495(04)74169-7 (literal)
Alternative label
  • Lorenzo Stella; Claudia Mazzuca; Mariano Venanzi; Antonio Palleschi; Mara Didonè; Fernando Formaggio; Claudio Toniolo; Basilio Pispisa (2004)
    Aggregation and Water-Membrane Partition as Major Determinants of the Activity of the Antibiotic Peptide Trichogin GA IV.
    in Biophysical journal (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Lorenzo Stella; Claudia Mazzuca; Mariano Venanzi; Antonio Palleschi; Mara Didonè; Fernando Formaggio; Claudio Toniolo; Basilio Pispisa (literal)
Pagina inizio
  • 936 (literal)
Pagina fine
  • 945 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 86 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento di Scienze e Tecnologie Chimiche, Università di Roma Tor Vergata, 00133 Rome, Italy; Istituto di Chimica Biomolecolare, Consiglio Nazionale delle Ricerche, Dipartimento di Chimica Organica, Università di Padova, 35131 Padua, Italy (literal)
Titolo
  • Aggregation and Water-Membrane Partition as Major Determinants of the Activity of the Antibiotic Peptide Trichogin GA IV. (literal)
Abstract
  • Water-membrane partition and aggregation behavior are fundamental aspects of the biological activity of antibiotic peptides, natural compounds causing the death of pathogenic organisms by perturbing the permeability of their membranes. A synthetic fluorescent analog of the natural lipopeptaibol trichogin GA IV was used to study its interaction with model membranes. Time-resolved fluorescence data show that in water, an equilibrium between monomers and small aggregates is present, the two species having different affinity for membranes. Therefore, association curves are strongly dependent on peptide concentration. A similar heterogeneity is present in the membrane phase, which strongly suggests the occurrence of a monomer-aggregate equilibrium in this case, too. The relative population of each species was determined and a strong correlation between the concentration of membrane-bound aggregates and membrane leakage was found, thereby suggesting that liposome perturbation is due to peptide aggregates only. Light-scattering measurements demonstrate that leakage is not due to liposome micellization. Moreover, experiments with markers of different sizes show that molecules with a diameter of similar to4 nm are released only to a minor extent. Overall, these results suggest that, within the concentration range explored, pore formation by peptide aggregates is the most likely mechanism of action for trichogin in membranes. (literal)
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