Partial thioamide scan on the lipopeptaibiotic trichogin GA IV. Effects on folding and bioactivity (Articolo in rivista)

Type
Label
  • Partial thioamide scan on the lipopeptaibiotic trichogin GA IV. Effects on folding and bioactivity (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.3762/bjoc.8.129 (literal)
Alternative label
  • Marta De Zotti; Barbara Biondi; Cristina Peggion; Matteo De Poli; Haleh Fathi; Simona Oancea; Claudio Toniolo; Fernando Formaggio (2012)
    Partial thioamide scan on the lipopeptaibiotic trichogin GA IV. Effects on folding and bioactivity
    in Beilstein journal of organic chemistry
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Marta De Zotti; Barbara Biondi; Cristina Peggion; Matteo De Poli; Haleh Fathi; Simona Oancea; Claudio Toniolo; Fernando Formaggio (literal)
Pagina inizio
  • 1161 (literal)
Pagina fine
  • 1171 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 8 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1. Univ Padua, CNR, Dept Chem, ICB,Padova Unit, I-35131 Padua, Italy 2. Lucian Blaga Univ Sibiu, Dept Biochem & Toxicol, Sibiu 550012, Romania (literal)
Titolo
  • Partial thioamide scan on the lipopeptaibiotic trichogin GA IV. Effects on folding and bioactivity (literal)
Abstract
  • Backbone modification is a common chemical tool to control the conformation of linear peptides and to explore potentially useful effects on their biochemical and biophysical properties. The thioamide, psi[CS-NH], group is a nearly isosteric structural mimic of the amide (peptide) functionality. In this paper, we describe the solution synthesis, chemical characterization, preferred conformation, and membrane and biological activities of three, carefully selected, peptide analogues of the lipopeptaibiotic [Leu(11)-OMe] trichogin GA IV. In each analogue, a single thioamide replacement was incorporated. Sequence positions near the N-terminus, at the center, and near the C-terminus were investigated. Our results indicate that (i) a thioamide linkage is well tolerated in the overall helical conformation of the [Leu(11)-OMe] lipopeptide analogue and (ii) this backbone modification is compatible with the preservation of its typical membrane leakage and antibiotic properties, although somewhat attenuated. (literal)
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