L- and D-amino acids form an amphipathic left-handed alpha-helix in the antibacterial lipodepsipeptide tolaasin (Articolo in rivista)

Type
Label
  • L- and D-amino acids form an amphipathic left-handed alpha-helix in the antibacterial lipodepsipeptide tolaasin (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Jourdan, F., Lazzaroni, S., López Méndez, B., de Julio, M., Lo Cantore, P., Amodeo, P., Iacobellis, N. S., Evidente, A. and MOTTA, A. (2003)
    L- and D-amino acids form an amphipathic left-handed alpha-helix in the antibacterial lipodepsipeptide tolaasin
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Jourdan, F., Lazzaroni, S., López Méndez, B., de Julio, M., Lo Cantore, P., Amodeo, P., Iacobellis, N. S., Evidente, A. and MOTTA, A. (literal)
Pagina inizio
  • 534 (literal)
Pagina fine
  • 543 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 52 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
  • F. Jourdan, post doc ICB; B. López Méndez, assegnista ICB; M. de Julio, laureanda ICB (literal)
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • L- and D-amino acids form an amphipathic left-handed alpha-helix in the antibacterial lipodepsipeptide tolaasin (literal)
Abstract
  • The 18-amino acid cytolytic lipodepsipeptide tolaasin, produced in culture by virulent strains of Pseudomonas tolaasii, is the causal agent of brown blotch disease of the cultivated mushroom. Its N-terminal region bears a sequence of D-amino acids, then alternate L- and D-amino acids, and a 5-residue C-terminal lactone ring. The solution structure of tolaasin in sodium dodecyl sulfate (SDS) was studied by resorting to NMR spectroscopy and molecular dynamics simulations. In SDS tolaasin forms an amphipathic left-handed a-helix in the region DPro2-DThr14 comprising the sequence of seven D-amino acids and the L-D-L-D-D-region. To the best of our knowledge, this is the first recognized example of a left-handed a-helix that includes both D- and L-amino acids. The lactone loop adopts a “boat-like” conformation and is shifted from the helical axis as to form a “golf-club” overall conformation. These structural features will be of importance in understanding, and preventing, tolaasin role in the bacterial colonization of the host plant, and its toxic action on cells. Furthermore, the observed antimicrobial activity together with the potential resistance to enzymatic degradation and the increased antigenicity (both due to the presence of L- and D-amino acids into the a-helix) suggests for tolaasin a potential role as a therapeutic antibacterial peptide. (literal)
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