Conformational Adaptation of β-Peptide Foldamers for the Formation of Metal-Peptide Frameworks

Metal-coordinated frameworks derived from small peptidic ligands have received much attention thanks to peptides' vast structural and functional diversity. Various peptides with partial conformational preferences have been used to build metal-peptide frameworks, however, the use of conformationally constrained beta-peptide foldamers has not been explored yet. Herein we report the first metal-coordination-mediated assembly of beta-peptide foldamers with 12-helical folding propensity. The coordination of Ag+ to the terminal pyridyl moieties afforded a set of metal-peptide frameworks with unique entangled topologies. Interestingly, formation of the network structures was accompanied by notable conformational distortions of the foldamer ligands. As the first demonstration of new metal-peptide frameworks built from modular beta-peptide foldamers, we anticipate that this work will be an important benchmark for further structural evolution and mechanistic investigation.

Automated summary

This study presents the first metal-coordination-mediated assembly of beta-peptide foldamers with 12-helical folding propensity, resulting in unique entangled metal-peptide frameworks. The formation of network structures is accompanied by notable conformational distortions of the foldamer ligands. This work is expected to be an important benchmark for further structural evolution and mechanistic investigation in the field of metal-peptide frameworks.