http://www.cnr.it/ontology/cnr/individuo/prodotto/ID210730
Folding of peptides characterized by c(3)Val, a highly constrained analogue of valine (Articolo in rivista)
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- Folding of peptides characterized by c(3)Val, a highly constrained analogue of valine (Articolo in rivista) (literal)
- Anno
- 2003-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/bip.10295 (literal)
- Alternative label
C. Peggion, F. Formaggio, M. Crisma, C. Toniolo, A.I. Jiménez, C. Cativiela, B. Kaptein, Q.B. Broxterman, M. Saviano, E. Benedetti (2003)
Folding of peptides characterized by c(3)Val, a highly constrained analogue of valine
in Biopolymers (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- C. Peggion, F. Formaggio, M. Crisma, C. Toniolo, A.I. Jiménez, C. Cativiela, B. Kaptein, Q.B. Broxterman, M. Saviano, E. Benedetti (literal)
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- Citazioni WOS: 7
Impact Factor 2003: 2.733
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- Institute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italy;
Department of Organic Chemistry, University of Zaragoza, 50009 Zaragoza, Spain;
DSM Fine Chemicals, Advanced Synthesis and Catalysis, 6160 MD Geleen, The Netherlands;
Institute of Biostructures and Bioimaging, CNR, Department of Chemistry, University of Naples, 80143 Naples, Italy (literal)
- Titolo
- Folding of peptides characterized by c(3)Val, a highly constrained analogue 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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