Measurement of acetylcholinesterase using a two‐dimensional electrochemical sensor LAAS

In this study, we measured the enzymatic activity of acetylcholinesterase (AChE) using the Light Addressable Amperometric Sensor (LAAS), an electrochemical sensor that can easily measure redox current values of multiple samples. Acetylthiocholine (ATCh) was used as a substrate. ATCh is hydrolyzed by...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Electronics and communications in Japan 2023-12, Vol.106 (4), p.n/a
Hauptverfasser: Miyairi, Akitsugu, Hasegawa, Yuki, Uchida, Hidekazu
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page n/a
container_issue 4
container_start_page
container_title Electronics and communications in Japan
container_volume 106
creator Miyairi, Akitsugu
Hasegawa, Yuki
Uchida, Hidekazu
description In this study, we measured the enzymatic activity of acetylcholinesterase (AChE) using the Light Addressable Amperometric Sensor (LAAS), an electrochemical sensor that can easily measure redox current values of multiple samples. Acetylthiocholine (ATCh) was used as a substrate. ATCh is hydrolyzed by AChE and releases electrons, making it possible to measure current values in accordance with the amount of substrate using LAAS. When KCl solution was used as the supporting electrolyte and an Ag/AgCl reference electrode as the counter electrode, a correlation between substrate concentration and reaction was confirmed in the range of 1 μM–10 mM. Malathion was then used as an inhibitor of AChE. Malathion phosphorylates and inactivates AChE, which prevents substrate hydrolysis and is expected to decrease the current value. Experimental results showed a decrease in sensor response correlated with inhibitor concentration.
doi_str_mv 10.1002/ecj.12425
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_2896054078</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2896054078</sourcerecordid><originalsourceid>FETCH-LOGICAL-c2785-74caee778a1300303e7e4b4c31bdd9b41c6ddf91532f9e830762f2b13a1ebbc53</originalsourceid><addsrcrecordid>eNp1kL1OwzAQxy0EEqUw8AaWmBjS-itxMlZV-VIRAzAwWY5zoa7SuNiJqm48As_Ik2AIYmO6O93vTn_9EDqnZEIJYVMw6wllgqUHaEQLwZIiFfTwr-f8GJ2EsCYkE6ngI_RyDzr0HjbQdtjVWBvo9o1Zuca2EDrwOgDug21fscbdzn2-f1Q2wsG6VjcYGjCdd2YFG2viHOLGebyczR5P0VGtmwBnv3WMnq8WT_ObZPlwfTufLRPDZJ4mUhgNIGWuKSeEEw4SRCkMp2VVFaWgJququqApZ3UBOScyYzUrKdcUytKkfIwuhr9b7976mFmtXe9juKBYXmQkFUTmkbocKONdCB5qtfV2o_1eUaK-zaloTv2Yi-x0YHe2gf3_oFrM74aLL-idcXA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2896054078</pqid></control><display><type>article</type><title>Measurement of acetylcholinesterase using a two‐dimensional electrochemical sensor LAAS</title><source>Wiley Online Library Journals Frontfile Complete</source><source>EBSCOhost Business Source Complete</source><creator>Miyairi, Akitsugu ; Hasegawa, Yuki ; Uchida, Hidekazu</creator><creatorcontrib>Miyairi, Akitsugu ; Hasegawa, Yuki ; Uchida, Hidekazu</creatorcontrib><description>In this study, we measured the enzymatic activity of acetylcholinesterase (AChE) using the Light Addressable Amperometric Sensor (LAAS), an electrochemical sensor that can easily measure redox current values of multiple samples. Acetylthiocholine (ATCh) was used as a substrate. ATCh is hydrolyzed by AChE and releases electrons, making it possible to measure current values in accordance with the amount of substrate using LAAS. When KCl solution was used as the supporting electrolyte and an Ag/AgCl reference electrode as the counter electrode, a correlation between substrate concentration and reaction was confirmed in the range of 1 μM–10 mM. Malathion was then used as an inhibitor of AChE. Malathion phosphorylates and inactivates AChE, which prevents substrate hydrolysis and is expected to decrease the current value. Experimental results showed a decrease in sensor response correlated with inhibitor concentration.</description><identifier>ISSN: 1942-9533</identifier><identifier>EISSN: 1942-9541</identifier><identifier>DOI: 10.1002/ecj.12425</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc</publisher><subject>acetylcholinesterase ; Chemical sensors ; drug screening ; Electrical measurement ; electrochemical imaging sensor ; Electrodes ; LAAS ; micro array ; Schottky junction ; Substrates</subject><ispartof>Electronics and communications in Japan, 2023-12, Vol.106 (4), p.n/a</ispartof><rights>2023 Wiley Periodicals LLC.</rights><rights>2023 by Wiley Periodicals LLC.</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2785-74caee778a1300303e7e4b4c31bdd9b41c6ddf91532f9e830762f2b13a1ebbc53</citedby><cites>FETCH-LOGICAL-c2785-74caee778a1300303e7e4b4c31bdd9b41c6ddf91532f9e830762f2b13a1ebbc53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fecj.12425$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fecj.12425$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27915,27916,45565,45566</link.rule.ids></links><search><creatorcontrib>Miyairi, Akitsugu</creatorcontrib><creatorcontrib>Hasegawa, Yuki</creatorcontrib><creatorcontrib>Uchida, Hidekazu</creatorcontrib><title>Measurement of acetylcholinesterase using a two‐dimensional electrochemical sensor LAAS</title><title>Electronics and communications in Japan</title><description>In this study, we measured the enzymatic activity of acetylcholinesterase (AChE) using the Light Addressable Amperometric Sensor (LAAS), an electrochemical sensor that can easily measure redox current values of multiple samples. Acetylthiocholine (ATCh) was used as a substrate. ATCh is hydrolyzed by AChE and releases electrons, making it possible to measure current values in accordance with the amount of substrate using LAAS. When KCl solution was used as the supporting electrolyte and an Ag/AgCl reference electrode as the counter electrode, a correlation between substrate concentration and reaction was confirmed in the range of 1 μM–10 mM. Malathion was then used as an inhibitor of AChE. Malathion phosphorylates and inactivates AChE, which prevents substrate hydrolysis and is expected to decrease the current value. Experimental results showed a decrease in sensor response correlated with inhibitor concentration.</description><subject>acetylcholinesterase</subject><subject>Chemical sensors</subject><subject>drug screening</subject><subject>Electrical measurement</subject><subject>electrochemical imaging sensor</subject><subject>Electrodes</subject><subject>LAAS</subject><subject>micro array</subject><subject>Schottky junction</subject><subject>Substrates</subject><issn>1942-9533</issn><issn>1942-9541</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNp1kL1OwzAQxy0EEqUw8AaWmBjS-itxMlZV-VIRAzAwWY5zoa7SuNiJqm48As_Ik2AIYmO6O93vTn_9EDqnZEIJYVMw6wllgqUHaEQLwZIiFfTwr-f8GJ2EsCYkE6ngI_RyDzr0HjbQdtjVWBvo9o1Zuca2EDrwOgDug21fscbdzn2-f1Q2wsG6VjcYGjCdd2YFG2viHOLGebyczR5P0VGtmwBnv3WMnq8WT_ObZPlwfTufLRPDZJ4mUhgNIGWuKSeEEw4SRCkMp2VVFaWgJququqApZ3UBOScyYzUrKdcUytKkfIwuhr9b7976mFmtXe9juKBYXmQkFUTmkbocKONdCB5qtfV2o_1eUaK-zaloTv2Yi-x0YHe2gf3_oFrM74aLL-idcXA</recordid><startdate>202312</startdate><enddate>202312</enddate><creator>Miyairi, Akitsugu</creator><creator>Hasegawa, Yuki</creator><creator>Uchida, Hidekazu</creator><general>Wiley Subscription Services, Inc</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SC</scope><scope>7SP</scope><scope>8FD</scope><scope>JQ2</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope></search><sort><creationdate>202312</creationdate><title>Measurement of acetylcholinesterase using a two‐dimensional electrochemical sensor LAAS</title><author>Miyairi, Akitsugu ; Hasegawa, Yuki ; Uchida, Hidekazu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2785-74caee778a1300303e7e4b4c31bdd9b41c6ddf91532f9e830762f2b13a1ebbc53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>acetylcholinesterase</topic><topic>Chemical sensors</topic><topic>drug screening</topic><topic>Electrical measurement</topic><topic>electrochemical imaging sensor</topic><topic>Electrodes</topic><topic>LAAS</topic><topic>micro array</topic><topic>Schottky junction</topic><topic>Substrates</topic><toplevel>online_resources</toplevel><creatorcontrib>Miyairi, Akitsugu</creatorcontrib><creatorcontrib>Hasegawa, Yuki</creatorcontrib><creatorcontrib>Uchida, Hidekazu</creatorcontrib><collection>CrossRef</collection><collection>Computer and Information Systems Abstracts</collection><collection>Electronics &amp; Communications Abstracts</collection><collection>Technology Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts – Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><jtitle>Electronics and communications in Japan</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Miyairi, Akitsugu</au><au>Hasegawa, Yuki</au><au>Uchida, Hidekazu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Measurement of acetylcholinesterase using a two‐dimensional electrochemical sensor LAAS</atitle><jtitle>Electronics and communications in Japan</jtitle><date>2023-12</date><risdate>2023</risdate><volume>106</volume><issue>4</issue><epage>n/a</epage><issn>1942-9533</issn><eissn>1942-9541</eissn><abstract>In this study, we measured the enzymatic activity of acetylcholinesterase (AChE) using the Light Addressable Amperometric Sensor (LAAS), an electrochemical sensor that can easily measure redox current values of multiple samples. Acetylthiocholine (ATCh) was used as a substrate. ATCh is hydrolyzed by AChE and releases electrons, making it possible to measure current values in accordance with the amount of substrate using LAAS. When KCl solution was used as the supporting electrolyte and an Ag/AgCl reference electrode as the counter electrode, a correlation between substrate concentration and reaction was confirmed in the range of 1 μM–10 mM. Malathion was then used as an inhibitor of AChE. Malathion phosphorylates and inactivates AChE, which prevents substrate hydrolysis and is expected to decrease the current value. Experimental results showed a decrease in sensor response correlated with inhibitor concentration.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc</pub><doi>10.1002/ecj.12425</doi><tpages>7</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1942-9533
ispartof Electronics and communications in Japan, 2023-12, Vol.106 (4), p.n/a
issn 1942-9533
1942-9541
language eng
recordid cdi_proquest_journals_2896054078
source Wiley Online Library Journals Frontfile Complete; EBSCOhost Business Source Complete
subjects acetylcholinesterase
Chemical sensors
drug screening
Electrical measurement
electrochemical imaging sensor
Electrodes
LAAS
micro array
Schottky junction
Substrates
title Measurement of acetylcholinesterase using a two‐dimensional electrochemical sensor LAAS
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-15T00%3A51%3A58IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Measurement%20of%20acetylcholinesterase%20using%20a%20two%E2%80%90dimensional%20electrochemical%20sensor%20LAAS&rft.jtitle=Electronics%20and%20communications%20in%20Japan&rft.au=Miyairi,%20Akitsugu&rft.date=2023-12&rft.volume=106&rft.issue=4&rft.epage=n/a&rft.issn=1942-9533&rft.eissn=1942-9541&rft_id=info:doi/10.1002/ecj.12425&rft_dat=%3Cproquest_cross%3E2896054078%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2896054078&rft_id=info:pmid/&rfr_iscdi=true