New tools for the control of peptide conformation and supramolecular chemistry: Crown-carrier, Cα-methyl L-DOPA amino acids
✍ Scribed by Fernando Formaggio; Simona Oancea; Cristina Peggion; Marco Crisma; Claudio Toniolo; Karen Wright; Michel Wakselman; Jean-Paul Mazaleyrat
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2003
- Tongue
- English
- Weight
- 186 KB
- Volume
- 71
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The preferred conformation of five, terminally protected, model peptide series to the hexamer level, based on three novel crowned, C^α^‐methyl L‐DOPA amino acids combined with either L‐Ala/Aib or Gly/Aib, were assessed in structure supporting solvents using FT‐IR absorption, ^1^H NMR, and CD techniques. The FT‐IR absorption spectra strongly suggest that the contribution of the crowned C^α^‐tetrasubstituted residue to intramolecular H‐bonding is equivalent to that of Aib and is much more significant than that of either L‐Ala or Gly. In addition, the ^1^H NMR titrations and the CD patterns resemble those typically exhibited by (right‐handed) 3~10~‐helical structures. © 2004 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2003