Metal-Coordinated Supramolecular Polymers from the Minimalistic Hybrid Peptide Foldamers.

Availing the peptide folded architectures to design metal-coordinated frameworks and cages is restricted due to the scarcity of readily accessible short and stable secondary structures. The secondary structures, α-helix and β-sheets, play significant roles in stabilizing tertiary folds of proteins. Designing such helical structures from the short sequences of peptides without having any steric restrictions is exceptionally challenging. Here we reveal the short α,γ-hybrid tripeptide sequences that manifest stable helical structures without having any sterically constrained amino acids. These short hybrid tripeptides fold into helices even in the presence of two typically β-sheet favoring Val residues. The hybrid helix consisting of terminal pyridine units coordinates with the metal ions and drives the helical polymerization. Depending on the sequence and the position of N in pyridine moieties, these peptides form selective metallogels with Ag+ and Cu2+ ions. The X-ray diffracted analysis of the peptide single crystals obtained from the gel matrix reveals that the helical structure is maintained during the self-assembly process. Further, by varying the counter anion, a 3D helical crystalline coordination polymer with permanent porosity is generated. The findings reported here can be used to design new functional metal-foldamer coordinated polymers.