A generally applicable method for assessing the electrophilicity and reactivity of diverse nitrile-containing compounds

Bioorg Med Chem Lett. 2007 Feb 15;17(4):998-1002. doi: 10.1016/j.bmcl.2006.11.044. Epub 2006 Nov 17.

Abstract

Nitrile-based inhibitors of cathepsin K have been known for some time and mechanism-of-action studies have demonstrated that cysteinyl proteases interact with nitriles in a reversible fashion. Three main classes of nitrile-containing inhibitors have been published in the cathepsin K field: (i) cyanamides, (ii) aromatic nitriles, and (iii) aminoacetonitriles. A computational approach was used to calculate the theoretical reactivities of diverse nitriles and this was found to correlate with their extent of reactivity with free cysteine. Moreover, there is a tentative link between high reactivity with cysteine and the potential to lead to irreversible covalent binding to proteins.

MeSH terms

  • Cathepsin K
  • Cathepsins / antagonists & inhibitors
  • Computational Biology
  • Cysteine / chemistry
  • Cysteine Proteinase Inhibitors / chemical synthesis*
  • Cysteine Proteinase Inhibitors / pharmacology
  • Electrochemistry
  • Humans
  • In Vitro Techniques
  • Indicators and Reagents
  • Microsomes, Liver / drug effects
  • Microsomes, Liver / enzymology
  • NADP / chemistry
  • Nitriles / chemistry*
  • Oxidation-Reduction

Substances

  • Cysteine Proteinase Inhibitors
  • Indicators and Reagents
  • Nitriles
  • NADP
  • Cathepsins
  • CTSK protein, human
  • Cathepsin K
  • Cysteine