N-Difluoromethyl-triazole as a constrained scaffold in peptidomimeticsElectronic supplementary information (ESI) available: Experimental procedures, NMR spectra. CCDC 1491960 (5c). For ESI and crystallographic data in CIF or other electronic format see DOI: 10.1039/c7cc01298e

The N -difluoromethyl triazolo-β-aza- -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...

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Main Authors: Mamone, M, Gonçalves, R. S. B, Blanchard, F, Bernadat, G, Ongeri, S, Milcent, T, Crousse, B
Format: Article
Language:English
Online Access:Get full text
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Summary:The N -difluoromethyl triazolo-β-aza- -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. The N -difluoromethyl triazolo-β-aza- -amino acid present in the core of peptides led to constrained conformations due to CH-F and NH-F interactions.
ISSN:1359-7345
1364-548X
DOI:10.1039/c7cc01298e