Docking studies and effects of syn-anti isomery of oximes derived from pyridine imidazol bicycled systems as potential human acetylcholinesterase reactivators
Identifikátory výsledku
Kód výsledku v 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>
Výsledek na webu
<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>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Docking studies and effects of syn-anti isomery of oximes derived from pyridine imidazol bicycled systems as potential human acetylcholinesterase reactivators
Popis výsledku v původním jazyce
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.
Název v anglickém jazyce
Docking studies and effects of syn-anti isomery of oximes derived from pyridine imidazol bicycled systems as potential human acetylcholinesterase reactivators
Popis výsledku anglicky
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.
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
FR - Farmakologie a lékárnická chemie
OECD FORD obor
—
Návaznosti výsledku
Projekt
—
Návaznosti
N - Vyzkumna aktivita podporovana z neverejnych zdroju
Ostatní
Rok uplatnění
2011
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Journal of Applied Biomedicine
ISSN
1214-021X
e-ISSN
—
Svazek periodika
9
Číslo periodika v rámci svazku
3
Stát vydavatele periodika
CZ - Česká republika
Počet stran výsledku
9
Strana od-do
163-171
Kód UT WoS článku
000291678000006
EID výsledku v databázi Scopus
—