Factors governing 3(10)-helix vs alpha-helix formation in peptides: percentage of C-alpha-tetrasubstituted alpha-amino acid residues and sequence dependence (Articolo in rivista)

Type
Label
  • Factors governing 3(10)-helix vs alpha-helix formation in peptides: percentage of C-alpha-tetrasubstituted alpha-amino acid residues and sequence dependence (Articolo in rivista) (literal)
Anno
  • 2002-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/bip.10178 (literal)
Alternative label
  • Crisma M., Bisson W., Formaggio F., Broxterman Q.B., Toniolo C. (2002)
    Factors governing 3(10)-helix vs alpha-helix formation in peptides: percentage of C-alpha-tetrasubstituted alpha-amino acid residues and sequence dependence
    in Biopolymers (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Crisma M., Bisson W., Formaggio F., Broxterman Q.B., Toniolo C. (literal)
Pagina inizio
  • 236 (literal)
Pagina fine
  • 245 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • Citazioni WOS: 19 Impact Factor 2002: 2.372 Primo autore (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 64 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italy; DSM Fine Chemicals, Advanced Synthesis and Catalysis, 6160 MD Geleen, The Netherlands (literal)
Titolo
  • Factors governing 3(10)-helix vs alpha-helix formation in peptides: percentage of C-alpha-tetrasubstituted alpha-amino acid residues and sequence dependence (literal)
Abstract
  • As an additional step toward the dissection of the factors responsible for the onset of 3(10)-helix vs alpha-helix in peptides, in this paper we describe the results of a three-dimensional (3D) structural analysis by x-ray diffraction of the N-alpha-acylated heptapeptide alkylamide mBrBz-L-Iva-L-(alphaMe)Val-L-Abu-L-(alphaMe)Val-L-(alphaMe)Phe-L-(alphaMe)Val-L-Iva-NHMe characterized by a single (L-Abu3) C-alpha-trisubstituted and six C-alpha-tetrasubstituted alpha-amino acids. We find that in the crystal state this peptide is folded in a mixed helical structure with short elements of 3(10)-helix at either terminus and a central region of alpha-helix. This finding, taken together with the published NMR and X-ray diffraction data on the all C-alpha-methylated parent sequence and its L-Val2 analog (also the latter heptapeptide has a single C-alpha-trisubstituted alpha-amino acid) strongly, supports the view that one C-alpha-trisubstituted alpha-amino acid inserted near the N-terminus of an N-alpha-acylated heptapeptide alkylamide sequence may be enough to switch a regular 3(10)-helix into an essentially alpha-helical conformation. As a corollary, of this work, the x-ray diffraction structure of the N-alpha-protected, C-terminal tetrapeptide alkylamide Z-L-(alphaMe)Val-L-(alphaMe)Phe-L-(alphaMe)Val-L-Iva-NHMe, also reported here, is clearly indicative of the preference of this fully C-alpha-methylated, short peptide for the 3(10)-helix. As the same terminally blocked sequence is mixed 3(10)/alpha-helical in the L-Abu3 heptapeptide amide but regular 3(10)-helical in the tetrapeptide amide and in the parent heptapeptide amide, these results point to an evident plasticity even of a fully C-alpha-methylated short peptide. (literal)
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