Nonpeptidic propargylamines as inhibitors of lysine specific demethylase 1 (LSD1) with cellular activity

J Med Chem. 2013 Sep 26;56(18):7334-42. doi: 10.1021/jm400792m. Epub 2013 Sep 5.

Abstract

Lysine demethylases play an important role in epigenetic regulation and thus in the development of diseases like cancer or neurodegenerative disorders. As the lysine specific demethylase 1 (LSD1/KDM1) has been strongly connected to androgen and estrogen dependent gene expression, it serves as a promising target for the therapy of hormone dependent cancer. Here, we report on the discovery of new small molecule inhibitors of LSD1 containing a propargylamine warhead, starting out from lysine containing substrate analogues. On the basis of these substrate mimicking inhibitors, we were able to increase potency by a combination of similarity-based virtual screening and subsequent synthetic optimization resulting in more druglike LSD1 inhibitors that led to histone hypermethylation in breast cancer cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amines / chemical synthesis
  • Amines / chemistry*
  • Amines / metabolism
  • Amines / pharmacology*
  • Animals
  • Cell Line, Tumor
  • Drug Design
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / metabolism
  • Enzyme Inhibitors / pharmacology*
  • Histone Demethylases / antagonists & inhibitors*
  • Histone Demethylases / chemistry
  • Histone Demethylases / metabolism
  • Histones / metabolism
  • Methylation / drug effects
  • Molecular Docking Simulation
  • Protein Conformation

Substances

  • Amines
  • Enzyme Inhibitors
  • Histones
  • Histone Demethylases
  • KDM1A protein, human