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

Unit of theoretical and structural physico-chemistry

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	4772-4776
Number of pages	5
Journal	Bioorganic & Medicinal Chemistry Letters
Volume	16
Issue number	18
DOIs	https://doi.org/10.1016/j.bmcl.2006.06.087
Publication status	Published - 15 Sept 2006

Keywords

(thio)Hydantoin
Binding mode
Crystallography
FAAH
Molecular modeling

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10.1016/j.bmcl.2006.06.087

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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",

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day = "15",

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

language = "English",

volume = "16",

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journal = "Bioorganic & Medicinal Chemistry Letters",

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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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DO - 10.1016/j.bmcl.2006.06.087

M3 - Article

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AN - SCOPUS:33747028750

SN - 0960-894X

VL - 16

SP - 4772

EP - 4776

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

Abstract

Keywords

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CCDC 606773: Experimental Crystal Structure Determination

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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

Abstract

Keywords

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Other files and links

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Datasets

CCDC 606773: Experimental Crystal Structure Determination

Cite this