2. Academic Validation
  3. Binding mode of new (thio)hydantoin inhibitors of fatty acid amide hydrolase: comparison with two original compounds, OL-92 and JP104

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

  • Bioorg Med Chem Lett. 2006 Sep 15;16(18):4772-6. doi: 10.1016/j.bmcl.2006.06.087.
Catherine Michaux 1,  Giulio G Muccioli,  Didier M Lambert,  Johan Wouters
Affiliations

Affiliation

  • 1 Drug Design and Discovery Center, FUNDP, 61 rue de Bruxelles, B-5000 Namur, Belgium. catherine.michaux@fundp.ac.be
PMID: 16844375 DOI: 10.1016/j.bmcl.2006.06.087
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.

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