Front Cover: Redox-Responsive Side Chain Structural Changes in a Seven-Membered Cyclic α,α-Disubstituted α-Amino Acid with a Disulfide Bond Enable Reversible Conformational Changes in Peptides (ChemPlusChem 4/2025)

Abstract

The front cover shows how redox-responsive side chain structural changes in amino acids enable reversible conformational transitions in peptides. Peptides incorporating cyclic amino acids with a disulfide adopt predominantly a well-defined 3₁₀-helical conformation in solution. In contrast, peptides containing acyclic amino acids with two thiol groups exhibit a diverse structural ensemble, consisting of both helical and non-helical conformations. More information can be found in the Research Article by Makoto Oba, Masakazu Tanaka, and co-workers (DOI: 10.1002/cplu.202400772).