Structure-Based Design of Selective LONP1 Inhibitors for Probing In Vitro Biology

J Med Chem. 2021 Apr 22;64(8):4857-4869. doi: 10.1021/acs.jmedchem.0c02152. Epub 2021 Apr 6.

Abstract

LONP1 is an AAA+ protease that maintains mitochondrial homeostasis by removing damaged or misfolded proteins. Elevated activity and expression of LONP1 promotes cancer cell proliferation and resistance to apoptosis-inducing reagents. Despite the importance of LONP1 in human biology and disease, very few LONP1 inhibitors have been described in the literature. Herein, we report the development of selective boronic acid-based LONP1 inhibitors using structure-based drug design as well as the first structures of human LONP1 bound to various inhibitors. Our efforts led to several nanomolar LONP1 inhibitors with little to no activity against the 20S proteasome that serve as tool compounds to investigate LONP1 biology.

MeSH terms

  • ATP-Dependent Proteases / antagonists & inhibitors*
  • ATP-Dependent Proteases / metabolism
  • Binding Sites
  • Boronic Acids / chemistry
  • Boronic Acids / metabolism
  • Boronic Acids / pharmacology
  • Bortezomib / chemistry
  • Bortezomib / metabolism
  • Cell Line
  • Cell Survival / drug effects
  • Drug Design*
  • Humans
  • Mitochondrial Proteins / antagonists & inhibitors*
  • Mitochondrial Proteins / metabolism
  • Molecular Docking Simulation
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / metabolism
  • Protease Inhibitors / pharmacology
  • Proteasome Endopeptidase Complex / chemistry
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Subunits / antagonists & inhibitors
  • Protein Subunits / metabolism
  • Structure-Activity Relationship

Substances

  • Boronic Acids
  • Mitochondrial Proteins
  • Protease Inhibitors
  • Protein Subunits
  • Bortezomib
  • ATP-Dependent Proteases
  • LONP1 protein, human
  • Proteasome Endopeptidase Complex