Reactivators of butyrylcholinesterase inhibited by organophosphorus compounds
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18470%2F24%3A50021580" target="_blank" >RIV/62690094:18470/24:50021580 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/00179906:_____/24:10481996
Výsledek na webu
<a href="https://www.sciencedirect.com/science/article/pii/S0045206824004310?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0045206824004310?via%3Dihub</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bioorg.2024.107526" target="_blank" >10.1016/j.bioorg.2024.107526</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Reactivators of butyrylcholinesterase inhibited by organophosphorus compounds
Popis výsledku v původním jazyce
In this review, the current progress in the research and development of butyrylcholinesterase (BChE) reactivators is summarised and the advantages or disadvantages of these reactivators are critically discussed. Organophosphorus compounds such as nerve agents (sarin, tabun, VX) or pesticides (chlorpyrifos, diazinon) cause irreversible inhibition of acetylcholinesterase (AChE) and BChE in the human body. While AChE inhibition can be life threatening due to cholinergic overstimulation and crisis, selective BChE inhibition has presumably no adverse effects. Because BChE is mostly found in plasma, its activity is important for the scavenging of organophosphates before they can reach AChE in the central nervous system. Therefore, this enzyme in combination with its reactivator can be used as a pseudo-catalytic scavenger of organophosphates. Three structural types of BChE reactivators were found, i.e. bisquaternary salts, monoquaternary salts and uncharged compounds. Although the reviewed reactivators have certain limitations, the promising candidates for BChE reactivation were found in each structural group.
Název v anglickém jazyce
Reactivators of butyrylcholinesterase inhibited by organophosphorus compounds
Popis výsledku anglicky
In this review, the current progress in the research and development of butyrylcholinesterase (BChE) reactivators is summarised and the advantages or disadvantages of these reactivators are critically discussed. Organophosphorus compounds such as nerve agents (sarin, tabun, VX) or pesticides (chlorpyrifos, diazinon) cause irreversible inhibition of acetylcholinesterase (AChE) and BChE in the human body. While AChE inhibition can be life threatening due to cholinergic overstimulation and crisis, selective BChE inhibition has presumably no adverse effects. Because BChE is mostly found in plasma, its activity is important for the scavenging of organophosphates before they can reach AChE in the central nervous system. Therefore, this enzyme in combination with its reactivator can be used as a pseudo-catalytic scavenger of organophosphates. Three structural types of BChE reactivators were found, i.e. bisquaternary salts, monoquaternary salts and uncharged compounds. Although the reviewed reactivators have certain limitations, the promising candidates for BChE reactivation were found in each structural group.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
30108 - Toxicology
Návaznosti výsledku
Projekt
<a href="/cs/project/GA22-14568S" target="_blank" >GA22-14568S: Biodistribuce a real-time monitoring volných nebo apoferitinem enkapsulovaných kvarterních reaktivátorů cholinesteras</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2024
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Bioorganic Chemistry
ISSN
0045-2068
e-ISSN
1090-2120
Svazek periodika
150
Číslo periodika v rámci svazku
September
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
19
Strana od-do
"Article Number: 107526"
Kód UT WoS článku
001256051200001
EID výsledku v databázi Scopus
2-s2.0-85195849686