Crystal Packing-induced Dimorphism of 12/10-Helical β-Peptides with Dynamic Folding Propensity

摘要

Conventional helical secondary structures in natural proteins adopt a single handedness arising from the stereochemistry of L-α-amino acid residues.1,2 In contrast, oligomers that consist of achiral residues may display both right-handed and left-handed conformations with rapid equilibrium.3,4 These dynamic helical peptide backbones have recently drawn much attention as scaffolds for stimuli-responsive functional oligomers, of which handedness may be switched reversibly by virtue of interaction with chiral molecules, solvent conditions, etc.4-7 The ratio between two opposite handed conformations can be measured by NMR and CD spectroscopic methods.