Controlled packing of metal–peptide superhelices with β-peptide foldamers

Abstract

Metal–peptide superhelices formed from 12/10-helical β-peptide foldamers exhibit programmable hierarchical assembly. A single metal-coordinated superhelix organizes into distinct parallel or antiparallel arrangements without conformational distortion. This adaptability arises from a minimized macrodipole and dynamic folding propensity, establishing general design principles for peptide-based supramolecular materials.