Cathepsin K inhibitors based on 2-amino-1,3,4-oxadiazole derivatives

Bioorg Chem. 2021 Apr:109:104662. doi: 10.1016/j.bioorg.2021.104662. Epub 2021 Jan 22.

Abstract

Two new series of hitherto unknown dipeptides, containing an electrophilic nitrile or a non-electrophilic 2-amino-1,3,4-oxadiazole moiety were synthesized and evaluated in vitro as Cathepsin K (Cat K) inhibitors. From 14 compounds obtained, the oxadiazole derivatives 10a, 10b, 10e, and 10g acted as enzymatic competitive inhibitors with Ki values between 2.13 and 7.33 µM. Molecular docking calculations were carried out and demonstrated that all inhibitors performed hydrogen bonds with residues from the enzyme active site, such as Asn18. The best inhibitors (10a, 10b, 10g) could also perform these bonds with Cys25, and 10a showed the most stabilizing interaction energy (-134.36 kcal mol-1) with the active cavity. For the first time, derivatives based in 2-amino-1,3,4-oxadiazole scaffolds were evaluated, and the results suggested that this core displays a remarkable potential as a building block for Cat K inhibitors.

Keywords: 1,3,4-Oxadiazoles; Cathepsin K; Dipeptides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Cathepsin K / antagonists & inhibitors*
  • Cell Survival / drug effects
  • Computer Simulation
  • Dipeptides / chemical synthesis
  • Dipeptides / chemistry
  • Dipeptides / pharmacology*
  • Drug Design
  • Human Umbilical Vein Endothelial Cells
  • Humans
  • Models, Molecular
  • Molecular Structure
  • Oxadiazoles / chemical synthesis
  • Oxadiazoles / chemistry
  • Oxadiazoles / pharmacology*
  • Protein Binding
  • Protein Conformation
  • Structure-Activity Relationship

Substances

  • Dipeptides
  • Oxadiazoles
  • Cathepsin K