Novel peptide foldameric motifs: a step forward in our understanding of the fully-extended conformation / 3(10)-helix coexistence (Articolo in rivista)

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Label
  • Novel peptide foldameric motifs: a step forward in our understanding of the fully-extended conformation / 3(10)-helix coexistence (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1039/c1ob06178j (literal)
Alternative label
  • Formaggio F.; Crisma M.; Ballano G.; Peggion C.; Venanzi M.; Toniolo C. (2012)
    Novel peptide foldameric motifs: a step forward in our understanding of the fully-extended conformation / 3(10)-helix coexistence
    in Organic & biomolecular chemistry
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Formaggio F.; Crisma M.; Ballano G.; Peggion C.; Venanzi M.; Toniolo C. (literal)
Pagina inizio
  • 2413 (literal)
Pagina fine
  • 2421 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 10 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1,2,3,4,6: ICB, Padova Unit, CNR, Department of Chemistry, University of Padova, 35131 Padova, Italy; 5: Department of Chemical Sciences and Technologies, University of Rome \"Tor Vergata\", 00133 Rome, Italy (literal)
Titolo
  • Novel peptide foldameric motifs: a step forward in our understanding of the fully-extended conformation / 3(10)-helix coexistence (literal)
Abstract
  • The fully-extended, multiple C-5, conformation or 2.0(5) helix is a very appealing peptide secondary structure, in particular for its potential use as a molecular spacer, as it is characterized by the longest elevation (as high as 3.62 angstrom) between the alpha-carbon atoms of two consecutive alpha-amino acids. Despite this intriguing property, however, it is only poorly investigated and understood. Here, using a complete series of C-alpha,C-alpha-diethylglycine (Deg) homo-oligopeptide esters to the pentamer level, we exploited the properties of a fluorophore and a quencher, synthetically positioned at the N- and C-termini of the main chain, respectively, to check the applicability of the fully-extended conformation as a rigid molecular spacer. The fluorescence study was complemented by FT-IR absorption and NMR conformational investigations. The X-ray diffraction structures of selected compounds are also reported. Unfortunately, we find that, even in a solvent of low polarity, such as chloroform, in this peptide series an equilibrium does take place between the fragile fully-extended conformation and the 3(10)-helical structure, the latter becoming more and more stable as the main chain is elongated. Since the Deg homo-peptide esters lacking any terminal aromatic group, previously investigated, are known to adopt a stable fully-extended conformation in chloroform solution, we tend to attribute the 3D-structure instability observed in this work to the presence of multiple aromatic rings in their blocking groups. (literal)
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