Synthesis, preferred conformation, protease stability, and membrane activity of heptaibin, a medium-length peptaibiotic (Articolo in rivista)

Type
Label
  • Synthesis, preferred conformation, protease stability, and membrane activity of heptaibin, a medium-length peptaibiotic (Articolo in rivista) (literal)
Anno
  • 2011-01-01T00:00:00+01:00 (literal)
Alternative label
  • De Zotti M., Biondi B., Peggion C., Park Y., Hahm K.S., Formaggio F., Toniolo C. (2011)
    Synthesis, preferred conformation, protease stability, and membrane activity of heptaibin, a medium-length peptaibiotic
    in Journal of peptide science (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • De Zotti M., Biondi B., Peggion C., Park Y., Hahm K.S., Formaggio F., Toniolo C. (literal)
Pagina inizio
  • 585 (literal)
Pagina fine
  • 594 (literal)
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  • 17 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Univ Padua, Dept Chem, CNR, ICB,Padova Unit, I-35131 Padua, Italy Chosun Univ, Dept Biotechnol, Sch Nat Sci, Kwangju 501759, South Korea (literal)
Titolo
  • Synthesis, preferred conformation, protease stability, and membrane activity of heptaibin, a medium-length peptaibiotic (literal)
Abstract
  • The medium-length peptaibiotics are characterized by a primary structure of 14-16 amino acid residues. Despite the interesting antibiotic and antifungal properties exhibited by these membrane-active peptides, their exact mechanism of action is still unknown. Here, we present our results on heptaibin, a 14-amino acid peptaibiotic found to exhibit antimicrobial activity against Staphylococcus aureus. We carried out the very challenging synthesis of heptaibin on solid phase and a detailed conformational analysis in solution. The peptaibiotic is folded in a mixed 3(10)-/alpha-helix conformation which exhibits a remarkable amphiphilic character. We also find that it is highly stable toward degradation by proteolytic enzymes and nonhemolytic. Finally, fluorescence leakage experiments using small unilamellar vesicles of three different compositions revealed that heptaibin, although uncharged, is a selective compound for permeabilization of model membranes mimicking the overall negatively charged surface of Gram-positive bacteria. This latter finding is in agreement with the originally published antimicrobial activity data. (literal)
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