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Journal Articles Organic & Biomolecular Chemistry Year : 2022

Two consecutive aza-amino acids in peptides promote stable β-turn formation in water

Abstract

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.
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Dates and versions

hal-03955106 , version 1 (24-01-2023)

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Chenghui Shi, Isabelle Correia, Nicolo Tonali, Sandrine Ongeri, Olivier Lequin. Two consecutive aza-amino acids in peptides promote stable β-turn formation in water. Organic & Biomolecular Chemistry, 2022, 20 (43), pp.8430-8437. ⟨10.1039/d2ob01225a⟩. ⟨hal-03955106⟩
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