Helix-loop-helix peptide foldamers and their use in the construction of hydrolase mimetics

Bioorg Chem. 2018 Dec:81:356-361. doi: 10.1016/j.bioorg.2018.07.012. Epub 2018 Jul 17.

Abstract

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.

Keywords: Catalysis; Circular dichroism; Conformation; Foldamers; Nuclear magnetic resonance; Peptides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biomimetic Materials / chemical synthesis
  • Biomimetic Materials / chemistry*
  • Catalysis
  • Helix-Loop-Helix Motifs
  • Hydrolases / chemistry
  • Hydrolysis
  • Kinetics
  • Peptides / chemical synthesis
  • Peptides / chemistry*
  • Protein Engineering
  • Protein Unfolding

Substances

  • Peptides
  • Hydrolases