Electrochemical detection of interaction between Thioflavin T and acetylcholinesterase

Vladimir Dounin, Andrea Constantinof, Holger Schulze, Till T Bachmann, Kagan Kerman

Research output: Contribution to journalArticlepeer-review


The electrochemical oxidation of the benzothiazole dye Thioflavin T (ThT) was found to be modulated by its interaction with electric eel acetylcholinesterase (AChE). Modifications of AChE by trace amounts of small molecule inhibitors such as carbachol and paraoxon were detectable electrochemically using minimal reagents and with greater sensitivity than attainable through conventional fluorescence approaches. This property appears to be unique to ThT, since its closely related neutral derivative BTA-1 only interacts with AChE, but is not significantly affected by the presence of small molecule inhibitors.
Original languageEnglish
Pages (from-to)1234-8
Number of pages5
Issue number6
Publication statusPublished - 2011


  • Acetylcholinesterase
  • Binding Sites
  • Carbachol
  • Cholinesterase Inhibitors
  • Electrochemical Techniques
  • Electrodes
  • Oxidation-Reduction
  • Paraoxon
  • Spectrometry, Fluorescence
  • Thiazoles


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