While peptides have demonstrated increasing interest as drugs, one major current issue is the design of small peptide analogues able to adopt preferential conformations, while possessing side chains similar to natural peptides in order to preserve their unique selectivity. We report in this article the synthesis and structural data based on experimental NMR conformational studies of peptides containing consecutive aza-amino acids. We demonstrate that a β-turn folding is induced by the introduction of one or two lateral chains on the diaza-peptide unit and that this folding is stable in aqueous media. This result is of particular importance for the design of peptidomimetics of biological interest. This work will be useful to investigate the ability of longer peptides containing these diaza-amino acids units to target protein-protein interactions (PPIs) involving turn or helical secondary structures or to stabilize the helical conformation of intrinsically disordered proteins (IDPs). PPIs and IDPs represent two of the most challenging drug discovery targets nowadays.