1: Bioorg Med Chem Lett. 2006 Sep 15;16(18):4772-6. Epub 2006 Jul 17.

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

Michaux C, Muccioli GG, Lambert DM, Wouters J.

Drug Design and Discovery Center, FUNDP, 61 rue de Bruxelles, B-5000 Namur,
Belgium; Laboratoire de Chimie Biologique Structurale, FUNDP, 61 rue de
Bruxelles, B-5000 Namur, Belgium.

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.

PMID: 16844375 [PubMed - in process]

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