α-Helix-to-β-sheet transitions in proteins have been implicated in a number of neurodegenerative diseases Several models based on switchable peptides to study these fundamental conformational changes have been developed. Switchable peptides are also of interest as new classes of dynamic nanomaterials. From a protein design perspective, stimulus-responsive peptides allow the study of noncovalent forces that control structure and dynamics of proteins and provide a platform for tuning protein function. Herein we describe the design of a redox-triggered peptide that rever-sibly switches conformations between a predominately α-helical state to a β-sheet aggregate. The peptide adopts a stable conformation in each state. Although several classes of switchable peptides have been described, a vast majority of these are irreversible (helix to sheet) or rely on non-biocompatible triggers, such as pH changes and/or thermal effects. Our design utilizes natural amino acid residues and mild triggers in physiological buffers, affording the opportunity to probe conformational changes in model proteins.
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