Thioether-derived Macrocycle for Peptide Secondary Structure Fixation

Abstract

Recently, we developed methods to stabilize peptides into various secondary structures, including α-helix, type III turn and β-hairpin via proper thioether based macrocyclization. These conformationally constrained peptidomimetics confer enhanced biophysical properties and provide a valuable avenue towards clinically-relevant therapeutic molecules. In this personal account, thioether-derived macrocyclization methods developed by our group for stabilization of α-helix, type-III β turn and β-hairpin conformations are discussed.

Keywords: constrained peptides; protein-protein interaction; type III β turn; α-helix; β-hairpin.