A Review of the Synthesis of Quaternary Acetylcholinesterase Reactivators
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18470%2F18%3A50014800" target="_blank" >RIV/62690094:18470/18:50014800 - isvavai.cz</a>
Alternative codes found
RIV/00179906:_____/18:10380717 RIV/60162694:G44__/18:43889582
Result on the web
<a href="http://www.eurekaselect.com/163684/article" target="_blank" >http://www.eurekaselect.com/163684/article</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.2174/1385272822666180711123529" target="_blank" >10.2174/1385272822666180711123529</a>
Alternative languages
Result language
angličtina
Original language name
A Review of the Synthesis of Quaternary Acetylcholinesterase Reactivators
Original language description
Acetylcholinesterase (AChE) is well-known enzyme studied in many fields of research, e.g. in Alzheimer’s disease, Parkinson’s disease, or in eco-toxicology as a biological marker. Many inhibitors of AChE have been identified in nature as well as prepared in chemical labs as a result of systematic synthetic efforts. The organophosphorus (OP) inhibitors of AChE are one of the oldest artificial inhibitors being purposely developed as military nerve agents (e.g. sarin, soman, tabun, VX, RVX). Some of the compounds with decreased toxicity are currently used in agriculture as pesticides (e.g. parathion, chlorpyrifos, paraoxon) or in the industry as softening agents and flame retardants. The common mechanism of action of all organophosphate compounds is the irreversible inhibition of AChE via a binding to the hydroxyl group of the serine residue within the active site of the enzyme. Subsequently, AChE loses its ability to fulfill its physiological role in cholinergic transmission, which leads to the cholinergic crisis with the possibility of respiratory failure and death. The reactivators of AChE are classified as strong nucleophilic agents capable to cleave the non-aged organophosphate-serine adduct and thereby restoring the activity of the enzyme. This work provides a unique overview of the most potent oximes reactivators of inhibited AChE since 1955 to the present. In this review article, we have reviewed different synthetic approaches of known and widely used oxime reactivators of AChE such as pralidoxime, methoxime, trimedoxime, obidoxime, asoxime (HI-6), HS-6, HLö-7, K027, K048, K203, K075 and BI-6. The review covers the original articles as well as patented research.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30107 - Medicinal chemistry
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Current organic chemistry
ISSN
1385-2728
e-ISSN
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Volume of the periodical
22
Issue of the periodical within the volume
16
Country of publishing house
AE - UNITED ARAB EMIRATES
Number of pages
30
Pages from-to
1619-1648
UT code for WoS article
000445405200004
EID of the result in the Scopus database
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