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Kuca, Kamil,Cabal, Jiri,Jung, Yung Sik,Musilek, Kamil,Soukup, Ondrej,Jun, Daniel,Pohanka, Miroslav,Musilova, Lucie,Karasová,, Jana,Novotný,, Ladislav,Hrabinova, Martina Blackwell Publishing Ltd 2009 Basic & clinical pharmacology & toxicology Vol.105 No.3
<P>Abstract: </P><P>Newly developed acetylcholinesterase reactivators K117 [1,5-bis(4-hydroxyiminomethylpyridinium)-3-oxapentane dichloride] and K127 [(1-(4-hydroxyiminomethylpyridinium)-5-(4-carbamoylpyridinium)-3-oxapentane dibromide)] were tested for their potency to reactivate tabun-inhibited human brain cholinesterases. Pralidoxime and trimedoxime were chosen as standard reference reactivators. Human tissue was used, as that was closer on the real treatment of human beings. As a result, oxime K127 was found as the best tested reactivator according to the constant <I>k</I><SUB>r</SUB>, characterizing the overall reactivation process. On the contrary, the maximal reactivation ability expressed as percentage of reactivation was the best for trimedoxime. This differences were caused as a result of using the enzyme from different species. Due to this, experiments on human tissue should be conducted after <I>in vitro</I> and <I>in vivo</I> tests on animals to eliminate such important failures of promising oximes.</P>
Ondrej Holas,Kamil Musilek,Miroslav Pohanka,Kamil Kuca,Veronika Opletalova,Young-Sik Jung 대한화학회 2010 Bulletin of the Korean Chemical Society Vol.31 No.6
Acetylcholinesterase reactivators are crucial antidotes for the treatment of organophosphate intoxication. Standard in vitro test was chosen using a rat brain homogenate as the source of AChE. Screening of reactivation potency was performed with two concentration of reactivator (1000 μM and 10 μM). Results were compared to established reactivators pralidoxime, methoxime, HI-6, trimedoxime and obidoxime. More than 30 novel reactivators performed equal or better reactivation ability of POX-inhibited AChE compared to currently used reactivators. The structure-activity relationship for reactivators of paraoxon-inhibited AChE was developed.
Holas, Ondrej,Musilek, Kamil,Pohanka, Miroslav,Kuca, Kamil,Opletalova, Veronika,Jung, Young-Sik Korean Chemical Society 2010 Bulletin of the Korean Chemical Society Vol.31 No.6
Acetylcholinesterase reactivators are crucial antidotes for the treatment of organophosphate intoxication. Standard in vitro test was chosen using a rat brain homogenate as the source of AChE. Screening of reactivation potency was performed with two concentration of reactivator (1000 ${\mu}M$ and 10 ${\mu}M$). Results were compared to established reactivators pralidoxime, methoxime, HI-6, trimedoxime and obidoxime. More than 30 novel reactivators performed equal or better reactivation ability of POX-inhibited AChE compared to currently used reactivators. The structure-activity relationship for reactivators of paraoxon-inhibited AChE was developed.
박노중,Young-Sik Jung*,Kamil Musilek,Daniel Jun,Kamil Kuca* 대한화학회 2006 Bulletin of the Korean Chemical Society Vol.27 No.9
Eight structurally different acetylcholinesterase reactivators derived from currently commercially available oximes were tested for their potency to reactivate acetylcholinesterase inhibited by pesticide paraoxon (P) and DFP (D). Housefly AChE (F) and bovine red blood cell AChE (B) were used as the source of the cholinesterases. Ellman's method was taken to examine cholinesterases activity. The results show that four AChE reactivators are potent AChE reactivators, able to reach reactivation potency of more than 30% in all cases - PF, PB, DF and DB. Their reactivation potency was comparable with that of pralidoxime and even higher compared with that of HI-6, standard AChE reactivators currently available on the market.
Park, No-Jung,Jung, Young-Sik,Musilek, Kamil,Jun, Daniel,Kuca, Kamil Korean Chemical Society 2006 Bulletin of the Korean Chemical Society Vol.27 No.9
Eight structurally different acetylcholinesterase reactivators derived from currently commercially available oximes were tested for their potency to reactivate acetylcholinesterase inhibited by pesticide paraoxon (P) and DFP (D). Housefly AChE (F) and bovine red blood cell AChE (B) were used as the source of the cholinesterases. Ellman's method was taken to examine cholinesterases activity. The results show that four AChE reactivators are potent AChE reactivators, able to reach reactivation potency of more than 30% in all cases - PF, PB, DF and DB. Their reactivation potency was comparable with that of pralidoxime and even higher compared with that of HI-6, standard AChE reactivators currently available on the market.
이상광,박민균,장호은,이진주,남기평,조대원,나춘섭,Kamil Musilek,Anna Horova,Jan Korabecny,Rafael Dolezal,Daniel Jun,Kamil Kuca* 대한화학회 2015 Bulletin of the Korean Chemical Society Vol.36 No.6
Novel types of symmetric bis-7-methoxytacrines connected by oligoethyleneoxy chains 3–5 and nonsymmetric monomeric 7-methoxytacrines containing hydroxyl-terminated oligoethyleneoxy chains 6–8 were prepared, and their in vitro/in silico effects on human recombinant AChE (hAChE) and human plasmatic butyrylcholinesterase (hBChE) were compared, with 7-MEOTA (2) as the standard compound. The symmetric bis-7-MEOTA derivatives 3–5 showed hAChE inhibition similar to that of 2. On the other hand, their effects on hBChE revealed an increasing inhibition trend when the oligoethyleneoxy units between the two 7-MEOTA moieties became longer. Accordingly, compounds 4 and 5 showed better selectivity towards hBChE. The most effective in the inhibition hAChE and hBChE was compound 8 with the longest oligoethyleneglycol chain, whereas compounds 6 and 7 resulted in similar IC50 values. A molecular modeling study using substrates 5 and 8 showed a possible binding conformation and protein–ligand interaction between the substrates and AChE/BChE.
Pohanka, Miroslav,Karasova, Jana Zdarova,Musilek, Kamil,Kuca, Kamil,Jung, Young-Sik,Kassa, Jiri Informa Healthcare 2011 Journal of enzyme inhibition and medicinal chemist Vol.26 No.1
<P>These experiments were performed on a rat model. The rats were divided into eight groups and consequently exposed to either a saline solution (control), atropine or a combination of atropine and tabun. The reactivation efficacy of the oximes was estimated on the rats exposed to tabun, atropine and a reactivator of AChE. The oximes HI-6, obidoxime, trimedoxime, K203 and KR-22836 were used as representative compounds of commonly available and new AChE reactivators. Besides the positive effect of the administered reactivators on blood AChE activity, the sizable modulation of low molecular weight antioxidant (LMWA) levels was also determined. The LMWA levels in the the animals treated with the oxime reactivators were decreased in comparison with the animals treated by atropine alone. It was found that the levels of LMWA returned to the level found in the control animals when either trimedoxime, K203 or KR-22836 were administered. The principle of oxime reactivator function and a novel insight into AChE activity regulation and oxidative stress is discussed.</P>