Crystal structure analysis of helix-turn-helix type motifs in α,γ-hybrid peptides

Abstract

Mimicking protein supersecondary structures using short synthetic peptide sequences holds significant importance in the fields of synthetic protein design, catalysis, and drug discovery. In this study, we present a series of helix–turn–helix motifs derived from short α,γ-hybrid peptides, incorporating centrally positioned E-α,β-unsaturated γ-amino acids. By varying the number of trans double bonds at the central residue, the positioning of the helices can be adjusted. Superimposing the synthetic seven-residue helix–turn–helix motif with the natural calcium-binding helix–turn–helix motif revealed the potential to design three-dimensional helix–turn–helix motifs within short peptide sequences.