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| Titel: |
Reactivation study of pyridinium oximes for acetylcholinesterases inhibited by paraoxon or DFP |
| Auteur: |
Tae-Hyuk Kim Kyung-Ae Oh No-Joong Park No-Sang Park Yeong Joon Kim Eul Kyun Yum Young-Sik Jung |
| Verschenen in: |
Journal of applied biomedicine |
| Paginering: | Jaargang 4 (2006) nr. 2 pagina's 67-72 |
| Jaar: |
2006 |
| Inhoud: |
We tested the potency to reactivate AChE inhibited by diisopropyl fluorophosphates (DFP) byusing bis-pyridinium oxime reactivators connected with CH2CH2OCH2CH2 linkers between twopyridinium rings. The potency was strongly dependent on oxime functional groups, and the bisoximederivatives 1,1-[Oxybis(ethylene)]-bis[4-(hydroxyimino)methyl]pyridinium dibromide (1)and 1,1-[Oxybis(ethylene)]-bis[2-(hydroxyimino)methyl]pyridinium dichloride (2) are more potentthan mono-oxime compounds 1-(4-hydroxyiminomethyl-1-pyridino)-5-(4-carbamoyl-1-pyridino)-3-oxapentane dibromide (3) and 1-(3-hydroxyiminomethyl-1-pyridino)-5-(4-carbamoyl-1-pyridino)-3-oxapentane dibromide (4). Not only is the number of oxime groups an importantstructural factor, but also their position. The in vitro reactivation ability of the most potent bispyridiniumoxime 2 was further evaluated for the housefly (HF) AChE inhibited by DFP and thebovine red blood cell (RBC) AChE inhibited by paraoxon. The reactivation ability of oxime 2 at5x10-3M concentration was almost 80% for HF-AChE inhibited by DFP and 82.1% for RBCAChEinhibited by paraoxon. |
| Uitgever: |
University of South Bohemia (provided by DOAJ) |
| Bronbestand: |
Elektronische Wetenschappelijke Tijdschriften |
Details van artikel 6 van 6 gevonden artikelen
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