Reprogramming Chirality in Peptide Self-Assembly via Intramolecular Side Chain-Backbone Hydrogen Bonding

While main chain-main chain and side chain-side chain interactions are known to maintain protein architectures, the role of main chain-side chain interactions remains largely unexplored. Among various amino acid side chains, uncharged polar ones may uniquely modulate molecular conformations through directional hydrogen bonding (H-bonding) with the main chain. Using 15 minimalistic amphiphilic peptides, we demonstrate that intrastrand H-bonding between C-terminal uncharged polar side chains and t