The preferred conformation of five, terminally protected, model peptide series to the hexamer level, based on three novel crowned, C-alpha-methyl L-DOPA amino acids combined with either L-Ala/Aib or Gly/Aib, were assessed in structure supporting solvents using FT-IR absorption, H-1 NMR, and CD techniques. The FT-IR absorption spectra strongly suggest that the contribution of the crowned C-alpha-tetrasubstituted residue to intramolecular H-banding is equivalent to that of Aib and is much more significant than that of either L-Ala or Gly. In addition, the H-1 NMR titrations and the CD patterns resemble those typically exhibited by (right-handed) 3(10)-helical structures.
New tools for the control of peptide conformation and supramolecular chemistry: crown-carrier, C-alpha-methyl L-DOPA amino acids
Crisma M;
2003
Abstract
The preferred conformation of five, terminally protected, model peptide series to the hexamer level, based on three novel crowned, C-alpha-methyl L-DOPA amino acids combined with either L-Ala/Aib or Gly/Aib, were assessed in structure supporting solvents using FT-IR absorption, H-1 NMR, and CD techniques. The FT-IR absorption spectra strongly suggest that the contribution of the crowned C-alpha-tetrasubstituted residue to intramolecular H-banding is equivalent to that of Aib and is much more significant than that of either L-Ala or Gly. In addition, the H-1 NMR titrations and the CD patterns resemble those typically exhibited by (right-handed) 3(10)-helical structures.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
