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A high throughput fluorescent assay for measuring the activity of fatty acid amide hydrolase.

Abstract：

:Fatty acid amide hydrolase (FAAH) is the enzyme responsible for the rapid degradation of fatty acid amides such as the endocannabinoid anandamide. Inhibition of FAAH activity has been suggested as a therapeutic approach for the treatment of chronic pain, depression and anxiety, through local activation of the cannabinoid receptor CB1. We have developed a high throughput screening assay for identification of FAAH inhibitors using a novel substrate, decanoyl 7-amino-4-methyl coumarin (D-AMC) that is cleaved by FAAH to release decanoic acid and the highly fluorescent molecule 7-amino-4-methyl coumarin (AMC). This assay gives an excellent signal window for measuring FAAH activity and, as a continuous assay, inherently offers improved sensitivity and accuracy over previously reported endpoint assays. The assay was validated using a panel of known FAAH inhibitors and purified recombinant human FAAH, then converted to a 384 well format and used to screen a large library of compounds (>600,000 compounds) to identify FAAH inhibitors. This screen identified numerous novel FAAH inhibitors of diverse chemotypes. These hits confirmed using a native FAAH substrate, anandamide, and had very similar rank order potency to that obtained using the D-AMC substrate. Collectively these data demonstrate that D-AMC can be successfully used to rapidly and effectively identify novel FAAH inhibitors for potential therapeutic use.

journal_name

J Neurosci Methods

journal_title

Journal of neuroscience methods

authors

Kage KL,Richardson PL,Traphagen L,Severin J,Pereda-Lopez A,Lubben T,Davis-Taber R,Vos MH,Bartley D,Walter K,Harlan J,Solomon L,Warrior U,Holzman TF,Faltynek C,Surowy CS,Scott VE

doi

10.1016/j.jneumeth.2006.10.006

subject

Has Abstract

pub_date

2007-03-30 00:00:00

pages

47-54

issue

1

eissn

0165-0270

issn

1872-678X

pii

S0165-0270(06)00505-X

journal_volume

161

pub_type

杂志文章

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