Synthesis and PGE₂ production inhibition of s-triazine derivatives as a novel scaffold in RAW 264.7 macrophage cells

Bioorg Med Chem Lett. 2014 Dec 1;24(23):5418-22. doi: 10.1016/j.bmcl.2014.10.031.

Abstract

We present the synthesis and biological evaluation of a collection of s-triazine derivatives as a novel scaffold of compounds with the capability to inhibit the PGE₂ production in LPS-induced RAW 264.7 macrophage cells. A total of 12 derivatives were synthesized and assayed for PGE₂ reduction at 10 μM concentration. Two compounds (7b and 7i) exhibiting >90% inhibition of PGE₂ production were found to have IC₅₀ values of 5.76 and 5.52 μM, respectively. They were counter screened for inhibition on COX-2 activity in a cell free assay. Specifically, compound 7i (R¹ = 4-Bn-Ph, R² = Cl, R³ = Ph, R⁵ = CO₂Me) was highly active in cells while maintaining little COX-2 inhibition (∼0% at 10 μM). Molecular docking study provides the possibility that compound 7i could inhibit PGE₂ production by blocking the PGH₂ binding site of mPGES-1 instead of COX-2 enzyme. Based on this result, our synthetic efforts will focus on intensive structure-activity relationship (SAR) study of s-triazine scaffold to discovery a potential PGE₂ synthesis inhibitor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Dinoprostone / antagonists & inhibitors
  • Dinoprostone / biosynthesis*
  • Inflammation / drug therapy
  • Inflammation / metabolism
  • Intramolecular Oxidoreductases / antagonists & inhibitors
  • Macrophages / drug effects*
  • Macrophages / metabolism
  • Mice
  • Prostaglandin-E Synthases
  • Structure-Activity Relationship
  • Triazines / chemical synthesis*
  • Triazines / chemistry
  • Triazines / pharmacology*

Substances

  • Triazines
  • Intramolecular Oxidoreductases
  • Prostaglandin-E Synthases
  • Ptges protein, mouse
  • Dinoprostone