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

doi:10.1016/j.bmcl.2006.06.087

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

Unite de recherche en chimie physique, theorique et structurale

Résultats de recherche: Contribution à un journal/une revue › Article › Revue par des pairs

Résumé

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.

langue originale	Anglais
Pages (de - à)	4772-4776
Nombre de pages	5
journal	Bioorganic & Medicinal Chemistry Letters
Volume	16
Numéro de publication	18
Les DOIs	https://doi.org/10.1016/j.bmcl.2006.06.087
Etat de la publication	Publié - 15 sept. 2006

Accès au document

10.1016/j.bmcl.2006.06.087

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Link to publication in Scopus

CCDC 606773: Experimental Crystal Structure Determination
Lambert, D. M. (Contributeur), Michaux, C. (Contributeur), Muccioli, G. (Contributeur) & Wouters, J. (Contributeur), Cambridge Crystallographic Data Centre, 1 janv. 2007
DOI: 10.5517/ccncdbq, http://www.ccdc.cam.ac.uk/services/structure_request?id=doi:10.5517/ccncdbq&sid=DataCite
Ensemble de données

Contient cette citation

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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.",

keywords = "(thio)Hydantoin, Binding mode, Crystallography, FAAH, Molecular modeling",

author = "Catherine Michaux and Muccioli, {Giulio G.} and Lambert, {Didier M.} and Johan Wouters",

year = "2006",

month = sep,

day = "15",

doi = "10.1016/j.bmcl.2006.06.087",

language = "English",

volume = "16",

pages = "4772--4776",

journal = "Bioorganic & Medicinal Chemistry Letters",

issn = "0960-894X",

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}

Binding mode of new (thio)hydantoin inhibitors of fatty acid amide hydrolase: Comparison with two original compounds, OL-92 and JP104. / Michaux, Catherine; Muccioli, Giulio G.; Lambert, Didier M. et al.
Dans: Bioorganic & Medicinal Chemistry Letters, Vol 16, Numéro 18, 15.09.2006, p. 4772-4776.

Résultats de recherche: Contribution à un journal/une revue › Article › Revue par des pairs

TY - JOUR

T1 - Binding mode of new (thio)hydantoin inhibitors of fatty acid amide hydrolase

T2 - Comparison with two original compounds, OL-92 and JP104

AU - Michaux, Catherine

AU - Muccioli, Giulio G.

AU - Lambert, Didier M.

AU - Wouters, Johan

PY - 2006/9/15

Y1 - 2006/9/15

N2 - 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.

AB - 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.

KW - (thio)Hydantoin

KW - Binding mode

KW - Crystallography

KW - FAAH

KW - Molecular modeling

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SN - 0960-894X

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JO - Bioorganic & Medicinal Chemistry Letters

JF - Bioorganic & Medicinal Chemistry Letters

IS - 18

ER -

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

Résumé

Accès au document

Autres fichiers et liens

Empreinte digitale

Ensembles de données

CCDC 606773: Experimental Crystal Structure Determination

Contient cette citation