Overcoming hERG issues for brain-penetrating cathepsin S inhibitors: 2-cyanopyrimidines. Part 2

Bioorg Med Chem Lett. 2008 Oct 1;18(19):5280-4. doi: 10.1016/j.bmcl.2008.08.067. Epub 2008 Aug 22.

Abstract

We describe here orally active and brain-penetrant cathepsin S selective inhibitors, which are virtually devoid of hERG K(+) channel affinity, yet exhibit nanomolar potency against cathepsin S and over 100-fold selectivity to cathepsin L. The new non-peptidic inhibitors are based on a 2-cyanopyrimidine scaffold bearing a spiro[3.5]non-6-yl-methyl amine at the 4-position. The brain-penetrating cathepsin S inhibitors demonstrate potential clinical utility for the treatment of multiple sclerosis and neuropathic pain.

MeSH terms

  • Administration, Oral
  • Animals
  • Brain / drug effects
  • Cathepsin L
  • Cathepsins / antagonists & inhibitors*
  • Combinatorial Chemistry Techniques
  • Cysteine Endopeptidases
  • Ether-A-Go-Go Potassium Channels / metabolism*
  • Humans
  • Male
  • Molecular Structure
  • Multiple Sclerosis / drug therapy
  • Pain / drug therapy
  • Pyrimidines / blood
  • Pyrimidines / chemical synthesis*
  • Pyrimidines / pharmacokinetics
  • Pyrimidines / pharmacology*
  • Rats
  • Rats, Sprague-Dawley
  • Structure-Activity Relationship

Substances

  • Ether-A-Go-Go Potassium Channels
  • Pyrimidines
  • Cathepsins
  • Cysteine Endopeptidases
  • CTSL protein, human
  • Cathepsin L
  • Ctsl protein, rat
  • cathepsin S