| Autor: |
Mamone M; Univ Paris-Sud, BioCIS, CNRS, Faculté de Pharmacie, 5 rue J-B. Clément, 92290 Châtenay-Malabry, France. benoit.crousse@u-psud.fr., Gonçalves RSB, Blanchard F, Bernadat G, Ongeri S, Milcent T, Crousse B |
| Jazyk: |
angličtina |
| Zdroj: |
Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2017 May 02; Vol. 53 (36), pp. 5024-5027. |
| DOI: |
10.1039/c7cc01298e |
| Abstrakt: |
The N-difluoromethyl triazolo-β-aza-ε-amino acid present in the core of peptides led to constrained conformations due to CH-F and NH-F interactions. Pseudotetrapeptides were obtained in excellent yields directly by click chemistry between azidodifluoroacetamides and alkynes, both linked to an amino acid. This work demonstrates that the N-difluoromethyltriazole scaffold can induce extended structures to β-strand mimics. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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