title: Characterization of the 310-helix in model peptides by HRMAS NMR spectroscopy.
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.
authors.affiliation: Institute of Chemistry, FRE 2446 CNRS-Bruker, Université Louis Pasteur, 67084 Strasbourg, France.
authors.forename: Nathalie
authors.initials: N
authors.lastname: Lancelot
authors.forename: Karim
authors.initials: K
authors.lastname: Elbayed
authors.forename: Jésus
authors.initials: J
authors.lastname: Raya
authors.forename: Martial
authors.initials: M
authors.lastname: Piotto
authors.forename: Jean-Paul
authors.initials: JP
authors.lastname: Briand
authors.forename: Fernando
authors.initials: F
authors.lastname: Formaggio
authors.forename: Claudio
authors.initials: C
authors.lastname: Toniolo
authors.forename: Alberto
authors.initials: A
authors.lastname: Bianco
mesh_terms: D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D010455:Peptides