Characterization of the 3-10-helix in model peptides by HRMAS NMR spectroscopy
| Autor: | Lancelot N., Elbayed K., Raya J., Piotto M., Briand J.P., Formaggio F., Toniolo C., Bianco A. |
|---|---|
| Rok vydání: | 2003 |
| Zdroj: | 9 (2003): 1317–1323. info:cnr-pdr/source/autori:Lancelot N., Elbayed K., Raya J., Piotto M., Briand J.P., Formaggio F., Toniolo C., Bianco A./titolo:Characterization of the 3-10-helix in model peptides by HRMAS NMR spectroscopy/doi:/rivista:/anno:2003/pagina_da:1317/pagina_a:1323/intervallo_pagine:1317–1323/volume:9 |
| Popis: | A tetra- and a hepta-homopeptide from the C-alpha-tetrasubstituted Aib (alpha-aminoisobutyric acid) residue were covalently linked to the POEPOP resin by the fragment-condensation approach. The conformational preferences of the two model peptides were determined for the first time on a solid support by means of high-resolution magic angle spinning NMR spectroscopy. The results obtained indicate that the Aib homopeptides adopt a regular 3(10)-helical structure even when they are covalently bound to a polymeric matrix, and thus confirm the remarkable conformational stability of the peptides rich in this amino acid. An ATR-FTIR spectroscopic investigation, performed in parallel, also confirmed that these polymer-bound peptides do indeed adopt a helical conformation. The results of this study open the possibility to exploit the peptide-resin conjugates based on C-alpha-tetrasubstituted a-amino acids as helpful, structurally organized templates in molecular recognition studies or as catalysts in asymmetric synthesis. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|