Identification of small molecules that selectively inhibit diacylglycerol lipase-α activity

J Biomol Screen. 2014 Apr;19(4):595-605. doi: 10.1177/1087057113511111. Epub 2013 Nov 15.

Abstract

Recent genetic evidence suggests that the diacylglycerol lipase (DAGL-α) isoform is the major biosynthetic enzyme for the most abundant endocannabinoid, 2-arachidonoyl-glycerol (2-AG), in the central nervous system. Revelation of its essential role in regulating retrograde synaptic plasticity and adult neurogenesis has made it an attractive therapeutic target. Therefore, it has become apparent that selective inhibition of DAGL-α enzyme activity with a small molecule could be a strategy for the development of novel therapies for the treatment of disease indications such as depression, anxiety, pain, and cognition. In this report, the authors present the identification of small-molecule inhibitor chemotypes of DAGL-α, which were selective (≥10-fold) against two other lipases, pancreatic lipase and monoacylglycerol lipase, via high-throughput screening of a diverse compound collection. Seven chemotypes of interest from a list of 185 structural clusters, which included 132 singletons, were initially selected for evaluation and characterization. Selection was based on potency, selectivity, and chemical tractability. One of the chemotypes, the glycine sulfonamide series, was prioritized as an initial lead for further medicinal chemistry optimization.

Keywords: 2-arachidonoyl-glycerol (2-AG); HTS; diacylglycerol lipase–α (DAGL-α); enzyme; inhibitor.

MeSH terms

  • Cell Line
  • Dose-Response Relationship, Drug
  • Drug Discovery*
  • Drug Evaluation, Preclinical / methods*
  • Enzyme Activation / drug effects
  • Enzyme Inhibitors / pharmacology*
  • High-Throughput Screening Assays
  • Humans
  • Kinetics
  • Lipoprotein Lipase / antagonists & inhibitors*
  • Lipoprotein Lipase / metabolism
  • Reproducibility of Results
  • Small Molecule Libraries*
  • Substrate Specificity

Substances

  • Enzyme Inhibitors
  • Small Molecule Libraries
  • DAGLA protein, human
  • Lipoprotein Lipase