Selective and brain-permeable polo-like kinase-2 (Plk-2) inhibitors that reduce α-synuclein phosphorylation in rat brain

ChemMedChem. 2013 Aug;8(8):1295-313. doi: 10.1002/cmdc.201300166. Epub 2013 Jun 21.

Abstract

Polo-like kinase-2 (Plk-2) has been implicated as the dominant kinase involved in the phosphorylation of α-synuclein in Lewy bodies, which are one of the hallmarks of Parkinson's disease neuropathology. Potent, selective, brain-penetrant inhibitors of Plk-2 were obtained from a structure-guided drug discovery approach driven by the first reported Plk-2-inhibitor complexes. The best of these compounds showed excellent isoform and kinome-wide selectivity, with physicochemical properties sufficient to interrogate the role of Plk-2 inhibition in vivo. One such compound significantly decreased phosphorylation of α-synuclein in rat brain upon oral administration and represents a useful probe for future studies of this therapeutic avenue toward the potential treatment of Parkinson's disease.

Keywords: Parkinson’s disease; computational chemistry; kinase inhibitors; medicinal chemistry; polo-like kinase-2.

MeSH terms

  • Animals
  • Binding Sites
  • Blood-Brain Barrier / metabolism
  • Brain / metabolism*
  • Female
  • HEK293 Cells
  • Half-Life
  • Humans
  • Male
  • Mice
  • Molecular Dynamics Simulation
  • Phosphorylation / drug effects
  • Protein Isoforms / antagonists & inhibitors
  • Protein Isoforms / metabolism
  • Protein Kinase Inhibitors / chemical synthesis
  • Protein Kinase Inhibitors / chemistry*
  • Protein Kinase Inhibitors / pharmacokinetics
  • Protein Serine-Threonine Kinases / antagonists & inhibitors*
  • Protein Serine-Threonine Kinases / metabolism
  • Protein Structure, Tertiary
  • Rats
  • Rats, Sprague-Dawley
  • alpha-Synuclein / metabolism*

Substances

  • Protein Isoforms
  • Protein Kinase Inhibitors
  • alpha-Synuclein
  • Protein Serine-Threonine Kinases
  • Plk2 protein, rat