American Chemical Society
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journal contribution
posted on 2008-11-07, 00:00 authored by Arnaud Salaün, Clémence Mocquet, Romain Perochon, Aurélien Lecorgne, Barbara Le Grel, Michel Potel, Philippe Le Grel
The cyclization of aza-β3-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 β3-cyclotetrapeptides. This folding property reduces considerably the polarity of aza-β3-tetrapeptides and should be useful in addressing intracellular targets.