De novo designed helix-loop-helix peptide foldamers containing cis-2-aminocyclopentanecarboxylic
acid residues were evaluated for their conformational stability and possible use in
enzyme mimetic development. The correlation between hydrogen bond network size and
conformational stability was demonstrated through CD and NMR spectroscopies. Molecules
incorporating a Cys/His/Glu triad exhibited enzyme-like hydrolytic activity.