Repurposing de novo designed entities reveals phosphodiesterase 3B and cathepsin L modulators

Chem Commun (Camb). 2015 May 1;51(35):7478-81. doi: 10.1039/c5cc01376c.

Abstract

Using computational bioactivity prediction models we identified phosphodiesterase 3B (PDE3B) and cathepsin L as macromolecular targets of de novo designed compounds. By disclosing the most potent cathepsin L activator known to date, small molecule repurposing by target panel prediction represents a feasible route towards innovative leads for chemical biology and molecular medicine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cathepsin L / antagonists & inhibitors
  • Cathepsin L / metabolism*
  • Computer Simulation
  • Cyclic Nucleotide Phosphodiesterases, Type 3 / chemistry
  • Cyclic Nucleotide Phosphodiesterases, Type 3 / metabolism*
  • Phosphodiesterase 3 Inhibitors / chemistry*
  • Phosphodiesterase 3 Inhibitors / metabolism
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / metabolism
  • Protein Binding
  • Structure-Activity Relationship

Substances

  • Phosphodiesterase 3 Inhibitors
  • Protease Inhibitors
  • Cyclic Nucleotide Phosphodiesterases, Type 3
  • Cathepsin L