Folding of peptides characterized by c3Val, a highly constrained analog of valine (Articolo in rivista)

Type
Label
  • Folding of peptides characterized by c3Val, a highly constrained analog of valine (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Peggion C., Formaggio F., Crisma M., Toniolo C., Jiménez A.I., Cativiela C., Kaptein B., Broxterman Q.B., Saviano M., Benedetti E. (2003)
    Folding of peptides characterized by c3Val, a highly constrained analog of valine
    in Biopolymers (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Peggion C., Formaggio F., Crisma M., Toniolo C., Jiménez A.I., Cativiela C., Kaptein B., Broxterman Q.B., Saviano M., Benedetti E. (literal)
Pagina inizio
  • 178 (literal)
Pagina fine
  • 191 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 68 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • Folding of peptides characterized by c3Val, a highly constrained analog of valine (literal)
Abstract
  • Using a combined chemical/chiral chromatographic approach we synthesized an N-protected derivative of (R)-c(3)Val, a severely conformationally restricted C-alpha-tetrasubstituted alpha-amino acid characterized by a C-beta,C-beta-dimethylated cyclopropane system. A set of terminally protected derivatives and model peptides (to the heptamer level), containing one or two (R)-c(3)Val residues in combination with either Aib or Gly residues, was prepared by solution methods. A detailed solution and crystal-state conformational investigation, based on Fourier transform infrared (FTIR) absorption, H-1-NMR, and x-ray diffraction techniques, performed in comparison with a similar study on related derivatives and peptides rich in (alphaMe)Val, the prototype of C-alpha-tetrasubstituted alpha-amino acids of this subfamily, allowed us to conclude the following: (a) c(3)Val is a good beta-bend and helix former, although less efficient than (alphaMe)Val. (b) The relationship between alpha-carbon chirality and screw sense of the folded structure formed is the same as that of (alphaMe) Val, i.e., the (R)-enantiomer has a strong left-handed bias. (c) c(3)Val seems more prone than (alphaMe)Val to fold into a gamma-bend conformation. The conformational propensities of C-beta,C-beta-disubstituted Ac(3)c residues are also discussed in comparison with those of the parent cyclopropane residue. (literal)
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