Electrochemical detection of interaction between Thioflavin T and acetylcholinesterase

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

doi:10.1039/c0an00743a

Electrochemical detection of interaction between Thioflavin T and acetylcholinesterase

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

Research output: Contribution to journal › Article › peer-review

Abstract / Description of output

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 language	English
Pages (from-to)	1234-8
Number of pages	5
Journal	Analyst
Volume	136
Issue number	6
DOIs	https://doi.org/10.1039/c0an00743a
Publication status	Published - 2011

Keywords / Materials (for Non-textual outputs)

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

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10.1039/c0an00743a

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title = "Electrochemical detection of interaction between Thioflavin T and acetylcholinesterase",

abstract = "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.",

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

author = "Vladimir Dounin and Andrea Constantinof and Holger Schulze and Bachmann, {Till T} and Kagan Kerman",

note = "This journal is {\textcopyright} The Royal Society of Chemistry 2011",

year = "2011",

doi = "10.1039/c0an00743a",

language = "English",

volume = "136",

pages = "1234--8",

journal = "Analyst",

issn = "0003-2654",

publisher = "Royal Society of Chemistry",

number = "6",

}

TY - JOUR

T1 - Electrochemical detection of interaction between Thioflavin T and acetylcholinesterase

AU - Dounin, Vladimir

AU - Constantinof, Andrea

AU - Schulze, Holger

AU - Bachmann, Till T

AU - Kerman, Kagan

N1 - This journal is © The Royal Society of Chemistry 2011

PY - 2011

Y1 - 2011

N2 - 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.

AB - 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.

KW - Acetylcholinesterase

KW - Binding Sites

KW - Carbachol

KW - Cholinesterase Inhibitors

KW - Electrochemical Techniques

KW - Electrodes

KW - Oxidation-Reduction

KW - Paraoxon

KW - Spectrometry, Fluorescence

KW - Thiazoles

UR - http://www.scopus.com/inward/record.url?scp=79952094894&partnerID=8YFLogxK

U2 - 10.1039/c0an00743a

DO - 10.1039/c0an00743a

M3 - Article

C2 - 21264414

SN - 0003-2654

VL - 136

SP - 1234

EP - 1238

JO - Analyst

JF - Analyst

IS - 6

ER -

Electrochemical detection of interaction between Thioflavin T and acetylcholinesterase

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