The Structural Distinction of α‐ and α,γ‐Hybrid Peptides Influences Their Zn(II)‐Coordinated Supramolecular Organization

The integration of protein secondary structures with metal ions offers a promising strategy for designing highly ordered self‐assembled structures with enhanced stability and functionality. The nature of the amino acids plays a crucial role in dictating the secondary structures of peptides. Here, we report highly stable and porous ZnCl 2 ‐helix‐frameworks from the α,γ‐hybrid peptide containing terminal 4‐pyridyl groups, whereas the control α‐peptide showed a ZnCl 2 ‐coordinated left‐handed superhelix network. The stable, porous 12‐helix frameworks of the α,γ‐hybrid peptide have been further explored as hosts to encapsulate guest solvent molecules such as nitromethane and 1,2‐dichloroethane after soaking the metal‐coordinated‐helix‐frameworks. Overall, the substitution of an α‐amino acid in a short α‐peptide sequence with a γ‐amino acid leads to a change in the helical structure as well as in its coordination ability.