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.

Characterization of the 310-Helix in Model Peptides by HRMAS NMR Spectroscopy

FORMAGGIO, FERNANDO;TONIOLO, CLAUDIO;
2003

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 a-amino acids as helpful, structurally organized templates in molecular recognition studies or as catalysts in asymmetric synthesis.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11577/2464515
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