A high-throughput TNP-ATP displacement assay for screening inhibitors of ATP-binding in bacterial histidine kinases

Assay Drug Dev Technol. 2011 Apr;9(2):174-83. doi: 10.1089/adt.2010.0289. Epub 2010 Nov 4.

Abstract

Bacterial histidine kinases (HK) are members of the GHKL superfamily, which share a unique adenosine triphosphate (ATP)-binding Bergerat fold. Our previous studies have shown that Gyrase, Hsp90, MutL (GHL) inhibitors bind to the ATP-binding pocket of HK and may provide lead compounds for the design of novel antibiotics targeting these kinases. In this article, we developed a competition assay using the fluorescent ATP analog, 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate. The method can be used for high-throughput screening of compound libraries targeting HKs or other ATP-binding proteins. We utilized the assay to screen a library of GHL inhibitors targeting the bacterial HK PhoQ, and discuss the applications of the 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate competition assay beyond GHKL inhibitor screening.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / analogs & derivatives*
  • Adenosine Triphosphate / antagonists & inhibitors
  • Adenosine Triphosphate / metabolism
  • High-Throughput Screening Assays / methods*
  • Histidine Kinase
  • Pharmaceutical Preparations* / chemistry
  • Pharmaceutical Preparations* / metabolism
  • Protein Binding / physiology
  • Protein Kinases / metabolism*
  • Random Allocation
  • Salmonella typhimurium / enzymology

Substances

  • Pharmaceutical Preparations
  • 2',3'-O-(2,4,6-trinitro-cyclohexadienylidine)adenosine 5'-triphosphate
  • Adenosine Triphosphate
  • Protein Kinases
  • Histidine Kinase