Characterization of the 310-helix in model peptides by HRMAS NMR spectroscopy |
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Authors: | Lancelot Nathalie Elbayed Karim Raya Jésus Piotto Martial Briand Jean-Paul Formaggio Fernando Toniolo Claudio Bianco Alberto |
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Affiliation: | Institute of Chemistry, FRE 2446 CNRS-Bruker, Université Louis Pasteur, 67084 Strasbourg, France. |
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Abstract: | 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 alpha-amino acids as helpful, structurally organized templates in molecular recognition studies or as catalysts in asymmetric synthesis. |
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Keywords: | conformation analysis 310‐helix HRMAS NMR spectroscopy peptides solid‐phase synthesis |
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