Molecular modeling and in vitro reactivation study between the oxime BI-6 and acetylcholinesterase inhibited by different nerve agents
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18450%2F15%3A50003670" target="_blank" >RIV/62690094:18450/15:50003670 - isvavai.cz</a>
Alternative codes found
RIV/00179906:_____/15:10296242
Result on the web
<a href="http://dx.doi.org/10.1080/07391102.2014.989408" target="_blank" >http://dx.doi.org/10.1080/07391102.2014.989408</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1080/07391102.2014.989408" target="_blank" >10.1080/07391102.2014.989408</a>
Alternative languages
Result language
angličtina
Original language name
Molecular modeling and in vitro reactivation study between the oxime BI-6 and acetylcholinesterase inhibited by different nerve agents
Original language description
Nerve agents are organophosphates acting as potent inhibitors of acetylcholinesterase (AChE), the enzyme responsible for the hydrolysis of acetylcholine and, consequently, the termination of the transmission of nerve impulses. The inhibition of AChE by an organophosphate can be reversed by a nucleophilic agent able to dephosphorylate a serine residue in the active site of AChE. In this sense, the oximes are compounds capable of removing the nerve agent and reactivate the enzyme. Here, we have applied amethodology involving theoretical docking and Quantum Mechanics/Molecular Mechanics, using the softwares Molegro(R) and Spartan(R), to evaluate the kinetic constants of reactivation and the interactions of the oxime BI-6 with AChE inhibited by differentorganophosphorus compounds in comparison to in vitro data. Results confirm that this method is suitable for the prediction of kinetic and thermodynamic parameters of oximes, which may be useful in the design and selection of new and more
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of biomolecular structure and dynamics
ISSN
0739-1102
e-ISSN
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Volume of the periodical
33
Issue of the periodical within the volume
9
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
2048-2058
UT code for WoS article
000358144400016
EID of the result in the Scopus database
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