Journal
JOURNAL OF APPLIED BIOMEDICINE
Volume 9, Issue 3, Pages 163-171Publisher
UNIV SOUTH BOHEMIA
DOI: 10.2478/v10136-009-0037-1
Keywords
acetylcholinesterase; docking studies; oximes; neurotoxic agents; theoretical calculation
Funding
- Brazilian financial agency CNPq
- Brazilian financial agency FAPERJ
- Brazilian financial agency FAPEMIG
- Brazilian financial agency CAPES/PRODEFESA
- Military Institute of Engineering for the physical infrastructure and working space
- Ministry of Defense (Czech Republic) [FVZUO0000604]
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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.
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