Binding mode of new (thio)hydantoin inhibitors of fatty acid amide hydrolase: Comparison with two original compounds, OL-92 and JP104

Catherine Michaux, Giulio G. Muccioli, Didier M. Lambert, Johan Wouters

Research output: Contribution to journalArticlepeer-review

Abstract

Substituted (thio)hydantoins (2-thioxoimidazolidinones and imidazolidinediones) were reported as new potential reversible inhibitors of fatty acid amide hydrolase (FAAH). Their binding mode to FAAH was explored to rationalize their activity and give idea to design highly active inhibitors. Starting from the crystal structure of one of these molecules, docking studies provide us with rational basis for the design of new inhibitors within the thiohydantoin family.

Original languageEnglish
Pages (from-to)4772-4776
Number of pages5
JournalBioorganic & Medicinal Chemistry Letters
Volume16
Issue number18
DOIs
Publication statusPublished - 15 Sep 2006

Keywords

  • (thio)Hydantoin
  • Binding mode
  • Crystallography
  • FAAH
  • Molecular modeling

Fingerprint

Dive into the research topics of 'Binding mode of new (thio)hydantoin inhibitors of fatty acid amide hydrolase: Comparison with two original compounds, OL-92 and JP104'. Together they form a unique fingerprint.

Cite this