title: Binding mode of new (thio)hydantoin inhibitors of fatty acid amide hydrolase: comparison with two original compounds, OL-92 and JP104.
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.
authors.affiliation: Drug Design and Discovery Center, FUNDP, 61 rue de Bruxelles, B-5000 Namur, Belgium. catherine.michaux@fundp.ac.be
authors.forename: Catherine
authors.initials: C
authors.lastname: Michaux
authors.forename: Giulio G
authors.initials: GG
authors.lastname: Muccioli
authors.forename: Didier M
authors.initials: DM
authors.lastname: Lambert
authors.forename: Johan
authors.initials: J
authors.lastname: Wouters
mesh_terms: D000581:Amidohydrolases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000737:chemistry*; D048289:Imidazolidines / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D013867:Thiohydantoins / Q000737:chemistry*; D000099252:Fatty Acid Amide Hydrolases
chemical_list: D000581:Amidohydrolases; D004791:Enzyme Inhibitors; D048289:Imidazolidines; D013867:Thiohydantoins; D000099252:Fatty Acid Amide Hydrolases; C514077:JP104 compound; C514076:OL-92 compound