Electrochemical Study on the Kinetic Behavior of the Immobilized Acetylcholinesterase

Stoytcheva, Margarita; Zlatev, Roumen; Velkova, Zdravka; Valdez, Benjamín; Ovalle, Marcela

doi:10.1149/1.3268385

ECS Trans.

2009

DOI: 10.1149/1.3268385

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Electrochemical Study on the Kinetic Behavior of the Immobilized Acetylcholinesterase

Margarita Stoytcheva¹,

Roumen Zlatev²,

Zdravka Velkova

et al.

Abstract: In this work are reported new results on the type of the immobilized acetylcholinesterase inhibition by specific and non-specific inhibitors, as well as the values of the characteristic enzyme reaction kinetic parameters in the absence and in the presence of inhibitors, identified applying an electrochemical approach.

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Cited by 2 publications

References 23 publications

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Some clinical applications of the electrochemical biosensors

Arredondo¹,

Stoytcheva²,

Zlatev³

et al. 2012

MRMC

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Electrochemical biosensing, due to its sensitivity and specificity, combined with the low-cost and operation convenience of the equipment, is considered as a promising point-of-care approach in clinical analysis. This review presents the basic principles of operation, the current status, and the trends in the development and the clinical implementation of some selected electrochemical biosensors. These include: electrochemical glucose biosensors successfully applied in diabetes management, and electrochemical biosensors for cholinesterases and trypsin activities determination. The latter, although less common, demonstrate the potential of improving the existing clinical methods in the diagnostics and the treatment of neurotoxic, neurological, and pancreatic diseases.

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Some clinical applications of the electrochemical biosensors

Arredondo¹,

Stoytcheva²,

Zlatev³

et al. 2012

MRMC

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Caffeine Inhibits Acetylcholinesterase, But Not Butyrylcholinesterase

Pohanka

Dobeš

2013

IJMS

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Caffeine is an alkaloid with a stimulant effect in the body. It can interfere in transmissions based on acetylcholine, epinephrine, norepinephrine, serotonin, dopamine and glutamate. Clinical studies indicate that it can be involved in the slowing of Alzheimer disease pathology and some other effects. The effects are not well understood. In the present work, we focused on the question whether caffeine can inhibit acetylcholinesterase (AChE) and/or, butyrylcholinesterase (BChE), the two enzymes participating in cholinergic neurotransmission. A standard Ellman test with human AChE and BChE was done for altering concentrations of caffeine. The test was supported by an in silico examination as well. Donepezil and tacrine were used as standards. In compliance with Dixon’s plot, caffeine was proved to be a non-competitive inhibitor of AChE and BChE. However, inhibition of BChE was quite weak, as the inhibition constant, Ki, was 13.9 ± 7.4 mol/L. Inhibition of AChE was more relevant, as Ki was found to be 175 ± 9 μmol/L. The predicted free energy of binding was −6.7 kcal/mol. The proposed binding orientation of caffeine can interact with Trp86, and it can be stabilize by Tyr337 in comparison to the smaller Ala328 in the case of human BChE; thus, it can explain the lower binding affinity of caffeine for BChE with reference to AChE. The biological relevance of the findings is discussed.

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Electrochemical Study on the Kinetic Behavior of the Immobilized Acetylcholinesterase

Cited by 2 publications

References 23 publications

Some clinical applications of the electrochemical biosensors

Some clinical applications of the electrochemical biosensors

Caffeine Inhibits Acetylcholinesterase, But Not Butyrylcholinesterase

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