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Int. J. Mol. Sci. 2013, 14(8), 16882-16900; doi:10.3390/ijms140816882

Oximes: Inhibitors of Human Recombinant Acetylcholinesterase. A Structure-Activity Relationship (SAR) Study

Received: 8 May 2013 / Revised: 1 August 2013 / Accepted: 2 August 2013 / Published: 16 August 2013
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Acetylcholinesterase (AChE) reactivators were developed for the treatment of organophosphate intoxication. Standard care involves the use of anticonvulsants (e.g., diazepam), parasympatolytics (e.g., atropine) and oximes that restore AChE activity. However, oximes also bind to the active site of AChE, simultaneously acting as reversible inhibitors. The goal of the present study is to determine how oxime structure influences the inhibition of human recombinant AChE (hrAChE). Therefore, 24 structurally different oximes were tested and the results compared to the previous eel AChE (EeAChE) experiments. Structural factors that were tested included the number of pyridinium rings, the length and structural features of the linker, and the number and position of the oxime group on the pyridinium ring.
Keywords: oximes; acetylcholinesterase; inhibitors; SAR study oximes; acetylcholinesterase; inhibitors; SAR study
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Sepsova, V.; Karasova, J.Z.; Korabecny, J.; Dolezal, R.; Zemek, F.; Bennion, B.J.; Kuca, K. Oximes: Inhibitors of Human Recombinant Acetylcholinesterase. A Structure-Activity Relationship (SAR) Study. Int. J. Mol. Sci. 2013, 14, 16882-16900.

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Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert