Cover Feature: Crystallography Reveals Metal‐Triggered Restructuring of β‐Hairpins (Chem. Eur. J. 59/2024)

β-Sheet peptides have long been pursued as ligands for bioinorganic chemistry. However, crystal structures of metal complexes with β-sheet peptides have remained elusive. By using a tryptophan zipper β-hairpin scaffold (12 amino acids), several histidine residues were incorporated to produce metal-binding peptides. Two Cu–β-sheet complexes were characterized by single-crystal X-ray crystallography and solution-phase measurements. The data reveal that Cu binding can trigger unexpected restructuring of the original hairpin structure into hairpin dimers and domain-swapped dimers, depending on the number and location of the histidine residues. More information can be found in the Research Article by A. I. Nguyen and co-workers (DOI: 10.1002/chem.202402101).