A poly(ADP-ribose) polymerase-1 activity assay based on the FRET between a cationic conjugated polymer and supercharged green fluorescent protein

Chem Commun (Camb). 2015 Oct 1;51(76):14389-92. doi: 10.1039/c5cc04170h. Epub 2015 Aug 14.

Abstract

A label-free and convenient strategy for PARP-1 activity assay and inhibitors assessment has been developed based on the fluorescence resonance energy transfer (FRET) between a cationic conjugated polymer (CCP) and supercharged green fluorescent protein (scGFP).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cations / chemistry
  • Cations / metabolism
  • Drug Evaluation, Preclinical / methods
  • Enzyme Assays / methods*
  • Fluorescence Resonance Energy Transfer / methods*
  • Green Fluorescent Proteins / chemistry*
  • Green Fluorescent Proteins / metabolism
  • Humans
  • Models, Molecular
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerase Inhibitors / pharmacology
  • Poly(ADP-ribose) Polymerases / analysis
  • Poly(ADP-ribose) Polymerases / blood
  • Poly(ADP-ribose) Polymerases / metabolism*
  • Poly(ADP-ribose) Polymerases / urine
  • Polymers / chemistry
  • Polymers / metabolism

Substances

  • Cations
  • Poly(ADP-ribose) Polymerase Inhibitors
  • Polymers
  • Green Fluorescent Proteins
  • PARP1 protein, human
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerases