Conformational analysis of TOAC-labelled alamethicin F50/5 analogues (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Conformational analysis of TOAC-labelled alamethicin F50/5 analogues (Articolo in rivista) (literal)

Anno

• 2007-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1002/cbdv.200790108 (literal)

Alternative label

• C. Peggion, M. Jost, Wim M. De Borggraeve, M. Crisma, F. Formaggio, C. Toniolo (2007)
  Conformational analysis of TOAC-labelled alamethicin F50/5 analogues
  in Chemistry & biodiversity (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• C. Peggion, M. Jost, Wim M. De Borggraeve, M. Crisma, F. Formaggio, C. Toniolo (literal)

Pagina inizio

• 1256 (literal)

Pagina fine

• 1268 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni

• Citazioni WOS: 7 Impact Factor 2007: 1.420 Coautore (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 4 (literal)

Rivista

• Chemistry & biodiversity (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Institute of Biomolecular Chemistry, Padova Unit, CNR, Department of Chemistry, University of Padova, 35131 Padova, Italy (literal)

Titolo

• Conformational analysis of TOAC-labelled alamethicin F50/5 analogues (literal)

Abstract

• In the preceding paper in this issue, we reported the total syntheses in solution of a set of four TOAC-containing analogues of the [(L)-Glu(OMe)(7.18.19)] F50/5 component of alamethicin, the prototype of peptaibol antibiotics forming channels in the biological membranes. In this article, we have expanded this work to the examination of their preferred conformation in solution by use of a combination of CD, FTIR absorption, and NMR spectroscopies. The results are strongly in favor of the view that replacement of the Aib residues at positions 1, 8, and 16 with TOAC (both are members of the helicogenic sub-class of C-alpha-tetrasubstituted alpha-amino acids) does not significantly affect the overwhelmingly populated a-helical 3D structure of alamethicin. The X-ray diffraction crystal structure of the N-alpha-protected, C-terminal, hexapeptide amide segment Z-(L)-Pro-(L)-Val-(Aib)(2)-[(L)-Glu(OMe)](2)-Fol lends further support to our conformational conclusions. (literal)

Prodotto di

• Peptidi antimicrobici e antivirali (PM.P01.013.001) (Modulo)
• Istituto di chimica biomolecolare (ICB) (Istituto)

Autore CNR

• CLAUDIO TONIOLO (Persona)
• FERNANDO FORMAGGIO (Unità di personale esterno)
• MARCO CRISMA (Unità di personale interno)

Incoming links:

Autore CNR di

• MARCO CRISMA (Unità di personale interno)
• CLAUDIO TONIOLO (Persona)
• FERNANDO FORMAGGIO (Unità di personale esterno)

Prodotto

• Istituto di chimica biomolecolare (ICB) (Istituto)
• Peptidi antimicrobici e antivirali (PM.P01.013.001) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Chemistry & biodiversity (Rivista)