The role of the oximes HI-6 and HS-6 inside human acetylcholinesterase inhibited with nerve agents: a computational study
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18470%2F18%3A50013773" target="_blank" >RIV/62690094:18470/18:50013773 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1080/07391102.2017.1389307" target="_blank" >http://dx.doi.org/10.1080/07391102.2017.1389307</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1080/07391102.2017.1389307" target="_blank" >10.1080/07391102.2017.1389307</a>
Alternative languages
Result language
angličtina
Original language name
The role of the oximes HI-6 and HS-6 inside human acetylcholinesterase inhibited with nerve agents: a computational study
Original language description
The oximes 4-carbamoyl-1-[({2-[(E)-(hydroxyimino) methyl] pyridinium-1-yl} methoxy) methyl] pyridinium (known as HI-6) and 3-carbamoyl-1-[({2-[(E)-(hydroxyimino) methyl] pyridinium-1-yl} methoxy) methyl] pyridinium (known as HS-6) are isomers differing from each other only by the position of the carbamoyl group on the pyridine ring. However, this slight difference was verified to be responsible for big differences in the percentual of reactivation of acetylcholinesterase (AChE) inhibited by the nerve agents tabun, sarin, cyclosarin, and VX. In order to try to find out the reason for this, a computational study involving molecular docking, molecular dynamics, and binding energies calculations, was performed on the binding modes of HI-6 and HS-6 on human AChE (HssAChE) inhibited by those nerve agents.
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
30108 - Toxicology
Result continuities
Project
—
Continuities
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
Journal of biomolecular structure and dynamics
ISSN
0739-1102
e-ISSN
—
Volume of the periodical
36
Issue of the periodical within the volume
13
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
3444-3452
UT code for WoS article
000455346900012
EID of the result in the Scopus database
2-s2.0-85032340388