Conformational Switch of Arylopeptide: Helix-Helix Transition Based on Side Chain Solvation

Controlling the structural transition between well-defined architectures found in living system is essential in polymer chemistry as well as material science. Herein, the reversible conformational switch of a non-natural polypeptide with an aromatic ring (2,6-naphthalene spacer) on its peptide backbone, referred to as an arylopeptide, between two distinct well-defined helical structures (extended 3₁ -helix and contracted 4₁ -helix) using side chain solvation is demonstrated. The folding selectivity of the arylopeptide and found that the affinity between the solvent and side chains is an essential factor for determining the global structure is investigated. A thermoresponsive arylopeptide bearing oligoether groups (─(CH₂ CH₂ O)₉ CH₃ )) on the side chain is designed, which exhibited unique lower critical solution temperature behavior and converted from the 3₁ to the 4₁ -helix depending on the temperature. Furthermore, the solvent affinity of the entire polymer by combining substituents (─(CH₂ CH₂ O)₃ CH₃ and ─C₁₂ H₂₅ ) with different properties on the side chains to achieve a spring-like expansion-contraction system that allows interconversion between 3₁ - and 4₁ -helices is adjusted.