17,20-lyase inhibitors. Part 4: design, synthesis and structure-activity relationships of naphthylmethylimidazole derivatives as novel 17,20-lyase inhibitors

Bioorg Med Chem. 2011 Mar 1;19(5):1751-70. doi: 10.1016/j.bmc.2011.01.017. Epub 2011 Jan 15.

Abstract

A novel series of naphthylmethylimidazole derivatives and related compounds have been investigated as selective 17,20-lyase inhibitors. Optimization of the substituent at the 6-position on the naphthalene ring was performed to yield a methylcarbamoyl derivative, which exhibited potent inhibitory activity against human 17,20-lyase and promising selectivity (>200-fold) for 17,20-lyase over CYP3A4. Further modifications of the methylcarbamoyl derivative led to the discovery of the corresponding tricyclic compound, which showed highly potent activity against human 17,20-lyase (IC(50) 19 nM) and good selectivity (>1000-fold) for inhibition of 17,20-lyase over CYP3A4. Additional biological evaluation revealed that the tricyclic compound had potent in vivo efficacy in monkeys and favorable pharmacokinetic profiles when administered in rats. Asymmetric synthesis of the selective tricyclic inhibitor was also achieved using a chiral α-hydroxy ketone.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cytochrome P-450 CYP3A / pharmacology
  • Drug Design*
  • Haplorhini
  • Humans
  • Imidazoles / chemical synthesis*
  • Imidazoles / chemistry
  • Imidazoles / pharmacology
  • Inhibitory Concentration 50
  • Lyases / antagonists & inhibitors*
  • Models, Molecular*
  • Molecular Structure
  • Naphthalenes / chemical synthesis*
  • Naphthalenes / chemistry*
  • Naphthalenes / pharmacology
  • Rats
  • Structure-Activity Relationship

Substances

  • Imidazoles
  • Naphthalenes
  • Cytochrome P-450 CYP3A
  • CYP3A4 protein, human
  • Lyases