Isovaline in Naturally Occurring Peptides: a Nondestructive Methodology for Configurational Assignment (Articolo in rivista)

Type
Label
  • Isovaline in Naturally Occurring Peptides: a Nondestructive Methodology for Configurational Assignment (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/bip.21679 (literal)
Alternative label
  • De Zotti M.; Biondi B.; Crisma M.; Hjørringgaard C.U.; Berg A.; Bruckner H.; Toniolo C. (2012)
    Isovaline in Naturally Occurring Peptides: a Nondestructive Methodology for Configurational Assignment
    in Biopolymers (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • De Zotti M.; Biondi B.; Crisma M.; Hjørringgaard C.U.; Berg A.; Bruckner H.; Toniolo C. (literal)
Pagina inizio
  • 36 (literal)
Pagina fine
  • 49 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 98 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
  • DOI: 10.1002/bip.21679 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1,2,3,7: Department of Chemistry, Institute of Biomolecular Chemistry, CNR, Padova Unit, University of Padova, 35131 Padova, Italy; 4: Department of Chemistry, The Center for Insoluble Protein Structures (in SPIN), Interdisciplinary Nanoscience Center, Aarhus University, 8000 Aarhus C, Denmark; 5: Department of Biomaterials, Innovent e.V., 07745 Jena, Germany; 6: Department of Food Sciences, Research Center for BioSystems, Land Use and Nutrition (IFZ), University of Giessen, 35392 Giessen, Germany (literal)
Titolo
  • Isovaline in Naturally Occurring Peptides: a Nondestructive Methodology for Configurational Assignment (literal)
Abstract
  • The nonproteinogenic, C-alpha-tetrasubstituted, helicogenic, chiral alpha-amino acid isovaline (Iva) is remarkably spread in the biosphere. Together with its achiral, lower homolog alpha-aminoisobutyric acid (Aib), it represents a characteristic marker of a class of naturally occurring peptide antibiotics, for which the acronym ''peptaibiotics'' became established. In these peptides, Iva occurs as the (S)-(= L) or the (R)-(= D) enantiomer, but peptide sequences containing both Iva enantiomers are also common. Here, we applied our recently developed 1-H NMR method, which enables the nondestructive assignment of the configuration of each Iva residue in a peptide of known helical screw sense, to natural and synthetic peptaibiotics. Our method proved to be generally applicable and provided evidence that, in the peptaibiotic bergofungin A, the Iva(12) configuration is (R) and not (S) as reported previously. Moreover, we extended our NMR method by including a 13-C-NMR parameter. A statistical analysis of the preferred main and side-chain conformations of the Iva residues in peptides, performed based on their published X-ray diffraction structures, allowed us to provide a sound rationale to the NMR criteria exploited to establish the configuration of this amino acid. (literal)
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