Docking studies and effects of syn-anti isomery of oximes derived from pyridine imidazol bicycled systems as potential human acetylcholinesterase reactivators
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00179906%3A_____%2F11%3A10118791" target="_blank" >RIV/00179906:_____/11:10118791 - isvavai.cz</a>
Result on the web
<a href="http://versita.metapress.com/content/313737828q533683/fulltext.pdf" target="_blank" >http://versita.metapress.com/content/313737828q533683/fulltext.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.2478/v10136-009-0037-1" target="_blank" >10.2478/v10136-009-0037-1</a>
Alternative languages
Result language
angličtina
Original language name
Docking studies and effects of syn-anti isomery of oximes derived from pyridine imidazol bicycled systems as potential human acetylcholinesterase reactivators
Original language description
In order to contribute to a better understanding of the mechanism of action of oximes, we evaluated the affinities of 10 new oximes, derived from pyridine-imidazol bicycled systems, for human acetylcholinesterase (HssAChE) complexed with tabun, by estimating their docking energy values and comparing of the values obtained to known oximes using the software Molegro Virtual Docker (MVD)(R). We evaluated the influence of the position of the oxime group as substituent in the structures and, also, the influence of the oxime group syn-anti isomery on the docking score values for all the molecules studied. Results suggest that: the affinities of the 10 new oximes for the tabun inhibited HssAChE active site are better than pralidoxime's and similar to trimedoxime's; the meta-pralidoxime could have more affinity for the HssAChE active site and the oximes' anti isomers could present slightly better affinities for the HssAChE active site than the syn isomers.
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
FR - Pharmacology and apothecary chemistry
OECD FORD branch
—
Result continuities
Project
—
Continuities
N - Vyzkumna aktivita podporovana z neverejnych zdroju
Others
Publication year
2011
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 Applied Biomedicine
ISSN
1214-021X
e-ISSN
—
Volume of the periodical
9
Issue of the periodical within the volume
3
Country of publishing house
CZ - CZECH REPUBLIC
Number of pages
9
Pages from-to
163-171
UT code for WoS article
000291678000006
EID of the result in the Scopus database
—