Different spectral signatures of octapeptide 3(10) and alpha-helices revealed by two-dimensional infrared spectroscopy (Articolo in rivista)

Type
Label
  • Different spectral signatures of octapeptide 3(10) and alpha-helices revealed by two-dimensional infrared spectroscopy (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/jp057472q (literal)
Alternative label
  • Hiroaki Maekawa; Claudio Toniolo; Alessandro Moretto; Quirinus B. Broxterman; Nien-Hui Ge (2006)
    Different spectral signatures of octapeptide 3(10) and alpha-helices revealed by two-dimensional infrared spectroscopy
    in The journal of physical chemistry. B
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Hiroaki Maekawa; Claudio Toniolo; Alessandro Moretto; Quirinus B. Broxterman; Nien-Hui Ge (literal)
Pagina inizio
  • 5834 (literal)
Pagina fine
  • 5837 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 110 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 12 (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Chemistry, University of California, Irvine, California, 92697-2025; Department of Chemistry, University of Padova, 35131 Padova, Italy; DSM Research, Life Sciences, Advanced Synthesis and Catalysis, P.O. Box 18, 6160 MD Geleen, The Netherlands (literal)
Titolo
  • Different spectral signatures of octapeptide 3(10) and alpha-helices revealed by two-dimensional infrared spectroscopy (literal)
Abstract
  • Femtosecond two-dimensional infrared (2D IR) spectroscopy is applied to the amide I modes of the terminally protected homo-octapeptide Z-[L-(alpha Me)Val](8)-OtBu in CDCl3, 2,2,2-trifluoroethanol (TFE), and 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) solutions to acquire 2D spectral signatures that distinguish between 3(10)- and alpha-helix structures. Suppression of diagonal peaks by controlling polarizations of IR pulses clearly reveals cross-peak patterns that are crucial for structural determination. A doublet feature is observed when the peptide ester forms a 3(10)-helix in CDCl3 and TFE and when it is at the initial stage of 3(10)- to alpha-helix transition in HFIP. In contrast, the 2D IR spectrum shows a multiple peak pattern after the peptide ester has acidolyzed and become an alpha-helix in HFIP. Electronic circular dichroism spectra accompanying the acidolysis-driven conformational change are also reported. This is the first report on the experimental 2D IR signature of a 3(10)-helical peptide. These results, using a model octapeptide, demonstrate the powerful capability of 2D IR spectroscopy to discriminate between different helical structures. (literal)
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