Electrochemical Biosensor for Markers of Neurological Esterase Inhibition

A novel, integrated experimental and modeling framework was applied to an inhibition-based bi-enzyme (IBE) electrochemical biosensor to detect acetylcholinesterase (AChE) inhibitors that may trigger neurological diseases. The biosensor was fabricated by co-immobilizing AChE and tyrosinase (Tyr) on t...

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Autores principales:	Neda Rafat, Paul Satoh, Robert Mark Worden
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	amperometric biosensor neural esterase acetylcholinesterase inhibition organophosphate design Biotechnology TP248.13-248.65
Acceso en línea:	https://doaj.org/article/934b319b540841728c9187e354c693aa
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spelling	oai:doaj.org-article:934b319b540841728c9187e354c693aa2021-11-25T16:55:41ZElectrochemical Biosensor for Markers of Neurological Esterase Inhibition10.3390/bios111104592079-6374https://doaj.org/article/934b319b540841728c9187e354c693aa2021-11-01T00:00:00Zhttps://www.mdpi.com/2079-6374/11/11/459https://doaj.org/toc/2079-6374A novel, integrated experimental and modeling framework was applied to an inhibition-based bi-enzyme (IBE) electrochemical biosensor to detect acetylcholinesterase (AChE) inhibitors that may trigger neurological diseases. The biosensor was fabricated by co-immobilizing AChE and tyrosinase (Tyr) on the gold working electrode of a screen-printed electrode (SPE) array. The reaction chemistry included a redox-recycle amplification mechanism to improve the biosensor’s current output and sensitivity. A mechanistic mathematical model of the biosensor was used to simulate key diffusion and reaction steps, including diffusion of AChE’s reactant (phenylacetate) and inhibitor, the reaction kinetics of the two enzymes, and electrochemical reaction kinetics at the SPE’s working electrode. The model was validated by showing that it could reproduce a steady-state biosensor current as a function of the inhibitor (PMSF) concentration and unsteady-state dynamics of the biosensor current following the addition of a reactant (phenylacetate) and inhibitor phenylmethylsulfonylfluoride). The model’s utility for characterizing and optimizing biosensor performance was then demonstrated. It was used to calculate the sensitivity of the biosensor’s current output and the redox-recycle amplification factor as a function of experimental variables. It was used to calculate dimensionless Damkohler numbers and current-control coefficients that indicated the degree to which individual diffusion and reaction steps limited the biosensor’s output current. Finally, the model’s utility in designing IBE biosensors and operating conditions that achieve specific performance criteria was discussed.Neda RafatPaul SatohRobert Mark WordenMDPI AGarticleamperometric biosensorneural esteraseacetylcholinesteraseinhibitionorganophosphatedesignBiotechnologyTP248.13-248.65ENBiosensors, Vol 11, Iss 459, p 459 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	amperometric biosensor neural esterase acetylcholinesterase inhibition organophosphate design Biotechnology TP248.13-248.65
spellingShingle	amperometric biosensor neural esterase acetylcholinesterase inhibition organophosphate design Biotechnology TP248.13-248.65 Neda Rafat Paul Satoh Robert Mark Worden Electrochemical Biosensor for Markers of Neurological Esterase Inhibition
description	A novel, integrated experimental and modeling framework was applied to an inhibition-based bi-enzyme (IBE) electrochemical biosensor to detect acetylcholinesterase (AChE) inhibitors that may trigger neurological diseases. The biosensor was fabricated by co-immobilizing AChE and tyrosinase (Tyr) on the gold working electrode of a screen-printed electrode (SPE) array. The reaction chemistry included a redox-recycle amplification mechanism to improve the biosensor’s current output and sensitivity. A mechanistic mathematical model of the biosensor was used to simulate key diffusion and reaction steps, including diffusion of AChE’s reactant (phenylacetate) and inhibitor, the reaction kinetics of the two enzymes, and electrochemical reaction kinetics at the SPE’s working electrode. The model was validated by showing that it could reproduce a steady-state biosensor current as a function of the inhibitor (PMSF) concentration and unsteady-state dynamics of the biosensor current following the addition of a reactant (phenylacetate) and inhibitor phenylmethylsulfonylfluoride). The model’s utility for characterizing and optimizing biosensor performance was then demonstrated. It was used to calculate the sensitivity of the biosensor’s current output and the redox-recycle amplification factor as a function of experimental variables. It was used to calculate dimensionless Damkohler numbers and current-control coefficients that indicated the degree to which individual diffusion and reaction steps limited the biosensor’s output current. Finally, the model’s utility in designing IBE biosensors and operating conditions that achieve specific performance criteria was discussed.
format	article
author	Neda Rafat Paul Satoh Robert Mark Worden
author_facet	Neda Rafat Paul Satoh Robert Mark Worden
author_sort	Neda Rafat
title	Electrochemical Biosensor for Markers of Neurological Esterase Inhibition
title_short	Electrochemical Biosensor for Markers of Neurological Esterase Inhibition
title_full	Electrochemical Biosensor for Markers of Neurological Esterase Inhibition
title_fullStr	Electrochemical Biosensor for Markers of Neurological Esterase Inhibition
title_full_unstemmed	Electrochemical Biosensor for Markers of Neurological Esterase Inhibition
title_sort	electrochemical biosensor for markers of neurological esterase inhibition
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/934b319b540841728c9187e354c693aa
work_keys_str_mv	AT nedarafat electrochemicalbiosensorformarkersofneurologicalesteraseinhibition AT paulsatoh electrochemicalbiosensorformarkersofneurologicalesteraseinhibition AT robertmarkworden electrochemicalbiosensorformarkersofneurologicalesteraseinhibition
_version_	1718412851515752448

Electrochemical Biosensor for Markers of Neurological Esterase Inhibition

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