New Foldamers: Rigid Peptides with an Alternating cis-trans Amide Sequence

Abstract

A review. The crystal-state structure of the terminally blocked homo-trimer from (2S,4R)-4-amino-5-oxopyrrolidine-2-carboxylic acid, characterized by a unique, alternating cis-trans amide sequence, was synthesized by the solid-phase technique and solved by X-ray diffraction. In the crystal packing mode the N-H and C=O groups of the trans peptide units were interconnected through either direct or water-mediated H-bonds. The computer modeling showed that the curved backbone led to the formation of a left-handed helical structure. [on SciFinder (R)]