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...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-11-01
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| Series: | Biosensors |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2079-6374/11/11/459 |
| _version_ | 1797511019327651840 |
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| author | Neda Rafat Paul Satoh Robert Mark Worden |
| author_facet | Neda Rafat Paul Satoh Robert Mark Worden |
| author_sort | Neda Rafat |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-10T05:40:25Z |
| format | Article |
| id | doaj.art-934b319b540841728c9187e354c693aa |
| institution | Directory Open Access Journal |
| issn | 2079-6374 |
| language | English |
| last_indexed | 2024-03-10T05:40:25Z |
| publishDate | 2021-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biosensors |
| spelling | doaj.art-934b319b540841728c9187e354c693aa2023-11-22T22:36:30ZengMDPI AGBiosensors2079-63742021-11-01111145910.3390/bios11110459Electrochemical Biosensor for Markers of Neurological Esterase InhibitionNeda Rafat0Paul Satoh1Robert Mark Worden2Department of Chemical Engineering and Materials Science, Michigan State University, 428 S. Shaw Lane, East Lansing, MI 48824, USADepartment of Chemical Engineering and Materials Science, Michigan State University, 428 S. Shaw Lane, East Lansing, MI 48824, USADepartment of Chemical Engineering and Materials Science, Michigan State University, 428 S. Shaw Lane, East Lansing, MI 48824, USAA 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.https://www.mdpi.com/2079-6374/11/11/459amperometric biosensorneural esteraseacetylcholinesteraseinhibitionorganophosphatedesign |
| spellingShingle | Neda Rafat Paul Satoh Robert Mark Worden Electrochemical Biosensor for Markers of Neurological Esterase Inhibition Biosensors amperometric biosensor neural esterase acetylcholinesterase inhibition organophosphate design |
| title | 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_short | Electrochemical Biosensor for Markers of Neurological Esterase Inhibition |
| title_sort | electrochemical biosensor for markers of neurological esterase inhibition |
| topic | amperometric biosensor neural esterase acetylcholinesterase inhibition organophosphate design |
| url | https://www.mdpi.com/2079-6374/11/11/459 |
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