2,6-Naphthyridines as potent and selective inhibitors of the novel protein kinase C isozymes

Bioorg Med Chem Lett. 2011 Dec 15;21(24):7367-72. doi: 10.1016/j.bmcl.2011.10.025. Epub 2011 Oct 21.

Abstract

The present study describes a novel series of ATP-competitive PKC inhibitors based on the 2,6-naphthyridine template. Example compounds potently inhibit the novel Protein Kinase C (PKC) isotypes δ, ε, η, θ (in particular PKCε/η, and display a 10-100-fold selectivity over the classical PKC isotypes. The prototype compound 11 was found to inhibit PKCθ-dependent pathways in vitro and in vivo. In vitro, a-CD3/a-CD28-induced lymphocyte proliferation could be effectively blocked in 10% rat whole blood. In mice, 11 dose-dependently inhibited Staphylococcus aureus enterotoxin B-triggered IL-2 serum levels after oral dosing.

MeSH terms

  • Administration, Oral
  • Animals
  • Binding Sites
  • Computer Simulation
  • Crystallography, X-Ray
  • Enterotoxins / toxicity
  • Interleukin-2 / blood
  • Isoenzymes / antagonists & inhibitors
  • Isoenzymes / metabolism
  • Mice
  • Naphthyridines / chemical synthesis
  • Naphthyridines / chemistry*
  • Naphthyridines / pharmacokinetics
  • Protein Kinase C / antagonists & inhibitors*
  • Protein Kinase C / metabolism
  • Protein Kinase Inhibitors / chemical synthesis
  • Protein Kinase Inhibitors / chemistry*
  • Protein Kinase Inhibitors / pharmacokinetics
  • Protein Structure, Tertiary
  • Rats
  • T-Lymphocytes / cytology
  • T-Lymphocytes / drug effects
  • T-Lymphocytes / immunology

Substances

  • Enterotoxins
  • Interleukin-2
  • Isoenzymes
  • Naphthyridines
  • Protein Kinase Inhibitors
  • enterotoxin B, staphylococcal
  • Protein Kinase C