Two consecutive aza-amino acids in peptides promote stable beta-turn formation in water
ORGANIC & BIOMOLECULAR CHEMISTRY(2022)
Abstract
Studies on the synthetic methodologies and the structural propensity of peptides containing consecutive aza-amino acids are still in their infancy. Here, details of the synthesis and conformational analysis of tripeptides containing two consecutive aza-amino acids are provided. The demonstration that the type I beta-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.
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