Superficially bound acetylcholinesterase based on a chitosan matrix for neurotoxiccCompound assay by a photographic technique
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F18%3A43889485" target="_blank" >RIV/60162694:G44__/18:43889485 - isvavai.cz</a>
Výsledek na webu
<a href="https://www.tandfonline.com/doi/abs/10.1080/00032719.2017.1381846?journalCode=lanl20" target="_blank" >https://www.tandfonline.com/doi/abs/10.1080/00032719.2017.1381846?journalCode=lanl20</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1080/00032719.2017.1381846" target="_blank" >10.1080/00032719.2017.1381846</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Superficially bound acetylcholinesterase based on a chitosan matrix for neurotoxiccCompound assay by a photographic technique
Popis výsledku v původním jazyce
Smartphones have become popular in the last decade and they have been used in analytical chemistry as easy detection systems with comparable parameters to standard laboratory equipment. This work focuses on the attachment of enzyme acetylcholinesterase on the previously activated chitosan. Acetylcholine splits the neurotransmitter acetylcholine, as a natural substrate, into choline and acetic acid. However, this compound can cleave alternative substrates, e.g., indoxyl acetate, which was used in this work. The conversion of the substrate is blocked or slowed down by inhibitors from which galantamine and tacrine were tested as model inhibitors with detection limits of 1.1 and 0.18 mu M, respectively. The measurement procedure was performed on a three-dimensional printed holder and red-green-blue channels were used for digital photography evaluation. The method was validated using a standard Ellman's spectrophotometric assay. We successfully attached acetylcholinesterase on the chitosan surface that was used for the inhibitor assay. The long-term stability of the immobilized enzyme as well as the sensitivity to organic solvents were also tested. The proposed method appeared to be suitable for the rapid and inexpensive assay of neurotoxic compounds.
Název v anglickém jazyce
Superficially bound acetylcholinesterase based on a chitosan matrix for neurotoxiccCompound assay by a photographic technique
Popis výsledku anglicky
Smartphones have become popular in the last decade and they have been used in analytical chemistry as easy detection systems with comparable parameters to standard laboratory equipment. This work focuses on the attachment of enzyme acetylcholinesterase on the previously activated chitosan. Acetylcholine splits the neurotransmitter acetylcholine, as a natural substrate, into choline and acetic acid. However, this compound can cleave alternative substrates, e.g., indoxyl acetate, which was used in this work. The conversion of the substrate is blocked or slowed down by inhibitors from which galantamine and tacrine were tested as model inhibitors with detection limits of 1.1 and 0.18 mu M, respectively. The measurement procedure was performed on a three-dimensional printed holder and red-green-blue channels were used for digital photography evaluation. The method was validated using a standard Ellman's spectrophotometric assay. We successfully attached acetylcholinesterase on the chitosan surface that was used for the inhibitor assay. The long-term stability of the immobilized enzyme as well as the sensitivity to organic solvents were also tested. The proposed method appeared to be suitable for the rapid and inexpensive assay of neurotoxic compounds.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10406 - Analytical chemistry
Návaznosti výsledku
Projekt
—
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2018
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Analytical Letters
ISSN
0003-2719
e-ISSN
—
Svazek periodika
51
Číslo periodika v rámci svazku
10
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
11
Strana od-do
1622-1632
Kód UT WoS článku
000429348300013
EID výsledku v databázi Scopus
2-s2.0-85044085562