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