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 ZnCl2-helix-frameworks from the α,γ-hybrid peptide containing terminal 4-pyridyl groups, whereas the control α-peptide showed a ZnCl2-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.