Characterization of binding properties of monoglyceride lipase inhibitors by a versatile fluorescence-based technique
| Autor: | Tapio Nevalainen, Juha R. Savinainen, Jarmo T. Laitinen, Megumi Yoshino, Anna Minkkilä |
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| Rok vydání: | 2009 |
| Předmět: |
Binding Sites
Binding properties Biophysics Serine hydrolase Cell Biology Biochemistry Fluorescence Endocannabinoid system Monoacylglycerol Lipases High-Throughput Screening Assays Monoacylglycerol lipase chemistry.chemical_compound Kinetics chemistry Glycerol Binding site Enzyme Inhibitors Molecular Biology JZL184 Enzyme Assays Fluorescent Dyes Protein Binding |
| Zdroj: | Analytical biochemistry. 399(1) |
| ISSN: | 1096-0309 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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