Turn Stabilization in Short Peptides by C-alpha-Methylated alpha-Amino Acids. (Articolo in rivista)

Type

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

Label

• Turn Stabilization in Short Peptides by C-alpha-Methylated alpha-Amino Acids. (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

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

• 10.1002/bip.20181 (literal)

Alternative label

• M. Crisma, A. Moretto, M. De Zotti, F. Formaggio, B. Kaptein, Q. B. Broxterman, C. Toniolo (2005)
  Turn Stabilization in Short Peptides by C-alpha-Methylated alpha-Amino Acids.
  in Biopolymers (Print)
  (literal)

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

• M. Crisma, A. Moretto, M. De Zotti, F. Formaggio, B. Kaptein, Q. B. Broxterman, C. Toniolo (literal)

Pagina inizio

• 279 (literal)

Pagina fine

• 293 (literal)

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

• Citazioni WOS: 12 Impact Factor 2005: 2.545 Corresponding author (literal)

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

• 80 (literal)

Rivista

• Biopolymers (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• Institute of Biomolecular Chemistry, CNR, Department of Chemistry, University of Padova, 35131 Padova, Italy; DSM Research, Life Sciences, Advanced Synthesis and Catalysis, 6160 MD Geleen, The Netherlands (literal)

Titolo

• Turn Stabilization in Short Peptides by C-alpha-Methylated alpha-Amino Acids. (literal)

Abstract

• The crystal-state conformations of three protected tripeptides, four tetrapeptides, and one pentapeptide, heavily based on the chiral C-alpha-methylated alpha-amino acids Iva, (alpha Me)Nva, and (Me) Val, were assessed by X-ray diffraction analyses. The eight peptide sequences are as follows: Z-((D)-Iva)(2)-(D)-Val-OMe, Z-(D)-Iva-(L)-Iva-Gly-OtBu, Z-(L)-Pro-(D)-Iva-(L)-Iva-Gly-OtBu, Z-(L)-Pro-(L)-Iva-(D)-Iva-Gly-OtBu, Z-Aib-[(L)-(alpha Me)Nva](2)-OtBu, Ac-[(L)-(alpha Me)Val](3)-D-(alpha Me)Val-OtBu, Z-[L-(alpha Me)Val](4)-OH, and Z-(L)-Ala-[(L)-(alpha Me)Nva](4)-OtBu. Two independent molecules were observed in the asymmetric units of Z-(D)-Iva-(L)-Iva-Gly-OtBu and Z-Aib-[(L)-(alpha Me)Nva](2)-OtBu, while three independent molecules were seen in Z-(L)-Ala-[(L)-(alpha Me)Nva](4)-OtBu. All peptides are folded in a single or multiple beta-turn conformations. Interestingly: (i) a water bridge within the N-terminal beta-turn is seen in Z-(L)-Pro-(L)-Iva-(D)-Iva-Gly-OtBu (dihydrate), and (ii) the hydroxyl group of the C-terminal carboxyl functionality of Z-[(L)-(alpha Me)Val](4)-OH generates an oxy-analogue of a beta-turn. The N-terminal beta-turn is missing in molecules A and B, but it does occur, although poorly stabilized, in molecule C, of Z-(L)-Ala-[(L)-(alpha Me)Nva](4)-OtBu. (literal)

Prodotto di

• Peptidi antimicrobici e antivirali (PM.P01.013.001) (Modulo)
• Institute of biomolecular chemistry (ICB) (Istituto)

Autore CNR

• MARCO CRISMA (Unità di personale interno)

Incoming links:

Autore CNR di

• MARCO CRISMA (Unità di personale interno)

Prodotto

• Institute of biomolecular chemistry (ICB) (Istituto)
• Peptidi antimicrobici e antivirali (PM.P01.013.001) (Modulo)

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

• Biopolymers (Rivista)