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 Sep 2006

Keywords

(thio)Hydantoin
Binding mode
Crystallography
FAAH
Molecular modeling

Access to Document

10.1016/j.bmcl.2006.06.087

Cite this

@article{a908b5842f864617a17012e6d1d64a12,

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 and medicinal chemistry letters",

issn = "0960-894X",

publisher = "Elsevier Limited",

number = "18",

}

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.; Wouters, Johan.

In: Bioorganic & Medicinal Chemistry Letters, Vol. 16, No. 18, 15.09.2006, p. 4772-4776.

Research output: Contribution to journal › Article › peer-review

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

UR - http://www.scopus.com/inward/record.url?scp=33747028750&partnerID=8YFLogxK

U2 - 10.1016/j.bmcl.2006.06.087

DO - 10.1016/j.bmcl.2006.06.087

M3 - Article

C2 - 16844375

AN - SCOPUS:33747028750

VL - 16

SP - 4772

EP - 4776

JO - Bioorganic and medicinal chemistry letters

JF - Bioorganic and medicinal chemistry letters

SN - 0960-894X

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

Access to Document

Other files and links

Fingerprint

CCDC 606773: Experimental Crystal Structure Determination

Cite this

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Datasets

CCDC 606773: Experimental Crystal Structure Determination

Cite this