Comprehensive Analysis of Structure-Activity Relationships of α-Ketoheterocycles as sn-1-Diacylglycerol Lipase α Inhibitors

J Med Chem. 2015 Dec 24;58(24):9742-53. doi: 10.1021/acs.jmedchem.5b01627. Epub 2015 Dec 2.

Abstract

Diacylglycerol lipase α (DAGLα) is responsible for the formation of the endocannabinoid 2-arachidonoylglycerol (2-AG) in the central nervous system. DAGLα inhibitors are required to study the physiological role of 2-AG. Previously, we identified the α-ketoheterocycles as potent and highly selective DAGLα inhibitors. Here, we present the first comprehensive structure-activity relationship study of α-ketoheterocycles as DAGLα inhibitors. Our findings indicate that the active site of DAGLα is remarkably sensitive to the type of heterocyclic scaffold with oxazolo-4N-pyridines as the most active framework. We uncovered a fundamental substituent effect in which electron-withdrawing meta-oxazole substituents increased inhibitor potency. (C6-C9)-acyl chains with a distal phenyl group proved to be the most potent inhibitors. The integrated SAR data was consistent with the proposed binding pose in a DAGLα homology model. Altogether, our results may guide the design of future DAGLα inhibitors as leads for molecular therapies to treat neuroinflammation, obesity, and related metabolic disorders.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases / antagonists & inhibitors
  • Databases, Chemical
  • HEK293 Cells
  • Humans
  • Ketones / chemistry*
  • Ketones / pharmacology
  • Lipoprotein Lipase / antagonists & inhibitors*
  • Lipoprotein Lipase / metabolism
  • Molecular Docking Simulation
  • Oxazoles / chemistry*
  • Oxazoles / pharmacology
  • Protein Binding
  • Pyridines / chemistry*
  • Pyridines / pharmacology
  • Structure-Activity Relationship

Substances

  • Ketones
  • Oxazoles
  • Pyridines
  • Lipoprotein Lipase
  • Amidohydrolases
  • fatty-acid amide hydrolase