Savinainen_2010_Anal.Biochem_399_132

Reference

Title : Characterization of binding properties of monoglyceride lipase inhibitors by a versatile fluorescence-based technique - Savinainen_2010_Anal.Biochem_399_132
Author(s) : Savinainen JR , Yoshino M , Minkkila A , Nevalainen T , Laitinen JT
Ref : Analytical Biochemistry , 399 :132 , 2010
Abstract :

Monoglyceride lipase (MGL) is a serine hydrolase that terminates the signaling of the primary endocannabinoid, 2-arachidonoyl glycerol (2-AG). Versatile high-throughput screening methods allowing the testing of MGL inhibitors are rare, thereby limiting the development and analysis of novel inhibitors. Here we describe an improved fluorescence-based technique that is capable of determining time- and dose-dependent inhibition of MGL with one or multiple binding sites and, at the same time, is capable of revealing the reversibility of inhibitor binding in a simple kinetic assay format. Known reference compounds as well as novel inhibitors, such as JZL184 and CAY10499, were evaluated for their MGL-binding properties and potency.

PubMedSearch : Savinainen_2010_Anal.Biochem_399_132
PubMedID: 20005861
Gene_locus related to this paper: human-MGLL

Related information

Inhibitor CAY10499    JZL184    MmPPOX
Gene_locus CAY10499    JZL184    MmPPOX    human-MGLL

Citations formats

Savinainen JR, Yoshino M, Minkkila A, Nevalainen T, Laitinen JT (2010)
Characterization of binding properties of monoglyceride lipase inhibitors by a versatile fluorescence-based technique
Analytical Biochemistry 399 :132

Savinainen JR, Yoshino M, Minkkila A, Nevalainen T, Laitinen JT (2010)
Analytical Biochemistry 399 :132