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Construction of an acetylcholinesterase sensor based on synthesized paramagnetic nanoparticles, a simple tool for neurotoxic compounds assay

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F17%3A43875750" target="_blank" >RIV/60162694:G44__/17:43875750 - isvavai.cz</a>

  • Alternative codes found

    RIV/62156489:43210/17:43911525 RIV/00216275:25310/17:39902675 RIV/00216305:26620/17:PU124060

  • Result on the web

    <a href="http://www.mdpi.com/1424-8220/17/4/676" target="_blank" >http://www.mdpi.com/1424-8220/17/4/676</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/s17040676" target="_blank" >10.3390/s17040676</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Construction of an acetylcholinesterase sensor based on synthesized paramagnetic nanoparticles, a simple tool for neurotoxic compounds assay

  • Original language description

    Magnetic particles (MPs) have been widely used in biological applications in recent years as a carrier for various molecules. Their big advantage is in repeated use of immobilized molecules including enzymes. Acetylcholinesterase (AChE) is an enzyme playing crucial role in neurotransmission and the enzyme is targeted by various molecules like Alzheimer&apos;s drugs, pesticides and warfare agents. In this work, an electrochemical biosensor having AChE immobilized onto MPs and stabilized through glutaraldehyde (GA) molecule was proposed for assay of the neurotoxic compounds. The prepared nanoparticles were modified by pure AChE and they were used for the measurement anti-Alzheimer&apos;s drug galantamine and carbamate pesticide carbofuran with limit of detection 1.5 mu M and 20 nM, respectively. All measurements were carried out using screen-printed sensor with carbon working, silver reference, and carbon auxiliary electrode. Standard Ellman&apos;s assay was used for validation measurement of both inhibitors. Part of this work was the elimination of reversible inhibitors represented by galantamine from the active site of AChE. For this purpose, we used a lower pH to get the original activity of AChE after inhibition by galantamine. We also observed decarbamylation of the AChE-carbofuran adduct. Influence of organic solvents to AChE as well as repeatability of measurement with MPs with AChE was also established.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30404 - Biomaterials (as related to medical implants, devices, sensors)

Result continuities

  • Project

    <a href="/en/project/LQ1601" target="_blank" >LQ1601: CEITEC 2020</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2017

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Sensors

  • ISSN

    1424-8220

  • e-ISSN

  • Volume of the periodical

    17

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    12

  • Pages from-to

    "neuvedeno"

  • UT code for WoS article

    000400822900017

  • EID of the result in the Scopus database

    2-s2.0-85016139336&doi