N-Methylation of N-alpha-acylated, fully C-alpha-methylated, linear, folded peptides: synthetic and conformational aspects (Articolo in rivista)

Type

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

Label

• N-Methylation of N-alpha-acylated, fully C-alpha-methylated, linear, folded peptides: synthetic and conformational aspects (Articolo in rivista) (literal)

Anno

• 2006-01-01T00:00:00+01:00 (literal)

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

• 10.1002/bip.20560 (literal)

Alternative label

• Moretto A., Crisma M., Kaptein B., Broxterman Q.B., Toniolo C. (2006)
  N-Methylation of N-alpha-acylated, fully C-alpha-methylated, linear, folded peptides: synthetic and conformational aspects
  in Biopolymers (Print)
  (literal)

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

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

Pagina inizio

• 553 (literal)

Pagina fine

• 565 (literal)

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

• Citazioni WOS: 8 Impact Factor 2006: 2.480 Coautore (literal)

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

• 84 (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

• N-Methylation of N-alpha-acylated, fully C-alpha-methylated, linear, folded peptides: synthetic and conformational aspects (literal)

Abstract

• Peptides characterized by single or multiple N-methylated, C-alpha-trisubstituted (e.g., protein) amino acids are of great interest in medicinal chemistry. Several naturally occurring peptides, remarkably stable to enzymatic attacks, are based on N-methylated residues. The classical conditions (CH3I/Ag2O in DMF, 24 h, room temperature) for N-methylation of the peptide function are useful tools for distinguishing solvent exposed from intramolecularly H-bonded -CO-NH-groups in peptides. In this work we have extended this reaction to N-alpha-acylated, linear peptides based exclusively on helicogenic C-alpha-tetrasubstituted alpha-amino acids, e.g., Aib (alpha-aminoisobutyric acid) or (alpha Me)Nva (C-alpha-methyl norvaline) residues. Under the experimental conditions used, only amide monomethylation (on the N-terminal, acylated, residue) takes place. Methylation of internal peptide groups linking two C-alpha-tetrasubstituted residues was not observed. Our FT-IR absorption, NMR, and X-ray diffraction investigations support the view that the beta-turn and 3(10)-helical conformations preferred by the original peptides are not dramatically perturbed in the derivatives mono-methylated at position 1. In particular, the tertiary amide bonds are trans. Conversely, the packing modes it? the crystals are strongly influenced by the reduction of the number of H-bonding donors. The MeXxx-Xxx peptide bond is readily disrupted under mild acidic conditions. (literal)

Prodotto di

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

Autore CNR

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

Incoming links:

Autore CNR di

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

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

• Biopolymers (Rivista)