Identification of indole inhibitors of human hematopoietic prostaglandin D2 synthase (hH-PGDS)

Bioorg Med Chem Lett. 2015 Jun 15;25(12):2496-500. doi: 10.1016/j.bmcl.2015.04.065. Epub 2015 Apr 28.

Abstract

Human H-PGDS has shown promise as a potential target for anti-allergic and anti-inflammatory drugs. Here we describe the discovery of a novel class of indole inhibitors, identified through focused screening of 42,000 compounds and evaluated using a series of hit validation assays that included fluorescence polarization binding, 1D NMR, ITC and chromogenic enzymatic assays. Compounds with low nanomolar potency, favorable physico-chemical properties and inhibitory activity in human mast cells have been identified. In addition, our studies suggest that the active site of hH-PGDS can accommodate larger structural diversity than previously thought, such as the introduction of polar groups in the inner part of the binding pocket.

Keywords: Focused screening; Hit validation; Indole; PGDS inhibitors; Prostaglandin D(2) synthase.

MeSH terms

  • Anti-Inflammatory Agents / chemical synthesis
  • Anti-Inflammatory Agents / chemistry
  • Anti-Inflammatory Agents / metabolism
  • Binding Sites
  • Crystallography, X-Ray
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / metabolism
  • Humans
  • Hydrogen Bonding
  • Indoles / chemical synthesis
  • Indoles / chemistry*
  • Indoles / metabolism
  • Intramolecular Oxidoreductases / antagonists & inhibitors*
  • Intramolecular Oxidoreductases / metabolism
  • Lipocalins / antagonists & inhibitors*
  • Lipocalins / metabolism
  • Molecular Dynamics Simulation
  • Protein Binding
  • Protein Structure, Tertiary
  • Structure-Activity Relationship

Substances

  • Anti-Inflammatory Agents
  • Enzyme Inhibitors
  • Indoles
  • Lipocalins
  • indole
  • Intramolecular Oxidoreductases
  • prostaglandin R2 D-isomerase