A new class of foldamers based on cis-gamma-amino-L-proline.
A synthetic method for the preparation of conformationally constrained gamma-peptides derived from gamma-amino-L-proline is described. The methodology allows the independent buildup of the peptide backbone and the introduction of sequential variations by reactions with the alpha-amino group of gamma-aminoproline. Both alkyl- and acyl-substituted gamma-peptides have been prepared and studied by CD and NMR. Conformational restrictions due to the cyclic structure of the monomer give rise to long-range interactions that are indicative of secondary structures even in aqueous solution. Interresidue NOEs suggest a concatenation of turns that, in a permissive solvent, could give rise to an isolated hydrogen bond ribbon, flanked and protected by proline rings.
Farrera-Sinfreu
Josep
J
Barcelona Biomedical Research Institute, Barcelona Science Park, University of Barcelona, Josep Samitier 1, 08028-Barcelona, Spain.
Zaccaro
Laura
L
Vidal
David
D
Salvatella
Xavier
X
Giralt
Ernest
E
Pons
Miquel
M
Albericio
Fernando
F
Royo
Miriam
M
D000613:Aminobutyrates / Q000737:chemistry; D002942:Circular Dichroism; D007202:Indicators and Reagents; D007536:Isomerism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry; D011392:Proline / Q000031:analogs & derivatives* / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D012997:Solvents
D000613:Aminobutyrates; D007202:Indicators and Reagents; D009842:Oligopeptides; D012997:Solvents; C467925:aminoproline; C005959:2,4-diaminobutyric acid; D011392:Proline