Two consecutive aza-amino acids in peptides promote stable β-turn formation in water
Résumé
Studies on the synthetic methodologies and the structural propensity of peptides containing consecutive aza-amino acids are still in their infancy. Here, the synthesis and conformational analysis of tripeptides containing two consecutive aza-amino acids are provided. The demonstration that the type I β-turn folding is induced, even in aqueous media, by the introduction of one or two lateral chains on the diaza-peptide unit is of particular importance for the design of peptidomimetics of biological interest.
Domaines
Chimie| Origine | Fichiers produits par l'(les) auteur(s) |
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