Aza-beta3-cyclotetrapeptides.
The cyclization of aza-beta(3)-tetrapeptides gives access to new CTP (cyclotetrapeptide) analogues. These stereocontrolled templates are assembled without any asymmetric synthesis. X-ray crystallographic structure and NMR analysis show that the macrocyclic scaffold is characterized by a fully cooperative intramolecular H-bond network, in sharp contrast with the nanotubular assemblies observed for beta(3)-cyclotetrapeptides. This folding property reduces considerably the polarity of aza-beta(3)-tetrapeptides and should be useful in addressing intracellular targets.
ICMV, UMR CNRS 6226, Université de Rennes I, 263 avenue du Général Leclerc, 35042 Rennes, Cedex, France.
Arnaud
A
Salaün
Clémence
C
Mocquet
Romain
R
Perochon
Aurélien
A
Lecorgne
Barbara
B
Le Grel
Michel
M
Potel
Philippe
P
Le Grel
D001372:Aza Compounds / Q000737:chemistry*; D018360:Crystallography, X-Ray; D003500:Cyclization; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides; D010456:Peptides, Cyclic / Q000138:chemical synthesis* / Q000737:chemistry
D001372:Aza Compounds; D009842:Oligopeptides; D010456:Peptides, Cyclic