A fluorescence-based assay for p38α recruitment site binders: identification of rooperol as a novel p38α kinase inhibitor

Chembiochem. 2013 Jan 2;14(1):66-71. doi: 10.1002/cbic.201200529. Epub 2012 Dec 6.

Abstract

A new p38α inhibitor: Using a D-recruitment site (DRS) probe for p38α which exploits covalent interaction with Cys119 and alkyne-azide "click" chemistry to identify small molecules that recognize the p38α DRS, the anti-inflammatory natural product rooperol was identified as a novel p38α inhibitor.

Publication types

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

MeSH terms

  • Binding Sites / drug effects
  • Catechols / metabolism*
  • Catechols / pharmacology*
  • Drug Evaluation, Preclinical
  • Imidazoles / chemical synthesis
  • Imidazoles / chemistry
  • Imidazoles / metabolism
  • Imidazoles / pharmacology
  • Models, Molecular
  • Phosphoproteins / antagonists & inhibitors
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism
  • Protein Binding
  • Protein Conformation
  • Protein Kinase Inhibitors / metabolism*
  • Protein Kinase Inhibitors / pharmacology*
  • Spectrometry, Fluorescence
  • Temperature
  • p38 Mitogen-Activated Protein Kinases / antagonists & inhibitors*
  • p38 Mitogen-Activated Protein Kinases / chemistry
  • p38 Mitogen-Activated Protein Kinases / metabolism*

Substances

  • Catechols
  • Imidazoles
  • Phosphoproteins
  • Protein Kinase Inhibitors
  • rooperol
  • p38 Mitogen-Activated Protein Kinases