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Kuca, Kamil,Jun, Daniel,Kim, Tae-Hyuk,Cabal, Jiri,Jung, Young-Sik Korean Chemical Society 2006 Bulletin of the Korean Chemical Society Vol.27 No.3
Nerve agents (sarin, tabun, soman and VX) are class of military important substances able to cause many severe intoxications during few minutes. Currently, the threat of misuse of these agents is daily discussed. Unfortunately, there is no single antidote able to treat intoxication caused by all of these agents. Owing to this fact, new generation of antidotes, especially acetylcholinesterase (AChE; EC 3.1.1.7) reactivators, is still developed. In this study, we have tested four newly developed AChE reactivators: 1-(4-hydroxyiminomethylpyridinium)- 5-(4-carbamoylpyridinium)-3-oxa-pentane dibromide (1), 1-(3-hydroxyiminomethylpyridinium)-5-(4-carbamoylpyridinium)-3-oxa-pentane dibromide (2), 1,5-bis(2-hydroxyiminomethylpyridinium)-3-oxa-pentane dichloride (3) and 1,5-bis(4-hydroxyiminomethylpyridinium)-3-oxa-pentane dibromide (4) for their potency to reactivate in vitro tabun and cyclosarin-inhibited AChE. Their reactivation efficacy was compared with currently the most promising oxime HI-6 (1-(2-hydroxyiminomethylpyridinium)-3-(4-carbamoylpyridinium)-2-oxa-propane dichloride). According to obtained results, two AChE reactivators 1 and 4 were able to reactivate tabun-inhibited AChE. On the contrary, there was no better AChE reactivator than HI-6 able to reactivate cyclosarin-inhibited AChE.
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>
Musilova, Lucie,Kuca, Kamil,Jung, Young-Sik,Jun, Daniel Taylor Francis 2009 Clinical toxicology Vol.47 No.6
<P>INTRODUCTION: Organophosphorus pesticides and nerve agents are highly toxic to humans and other living organisms, primarily because of their interaction with enzyme acetylcholinesterase. The aim of our study was to find suitable reactivators of acetylcholinesterase and butyrylcholinesterase and to recommend the most efficacious compounds for the next evaluation as antidotes for intoxication by pesticides. METHODS: Eighteen structurally different oxime reactivators were tested for their in vitro ability to reactivate paraoxon-inhibited human erythrocyte acetylcholinesterase and human plasma butyrylcholinesterase to find out structure-activity relationship within this set of compounds. Their reactivation ability was compared with commercially available acetylcholinesterase reactivators (pralidoxime, methoxime, trimedoxime, obidoxime, and HI-6). RESULTS AND DISCUSSION: The best reactivation ability was achieved with obidoxime, trimedoxime, compounds K027, K075, K203, and K048. We have also tested reactivation of butyrylcholinesterase with the aim to recommend an efficient reactivator, able to perform a 'pseudo catalytic' bioscavenger with butyrylcholinesterase, which is developed as new antidote of organophosphate poisonings. Such combination could allow an enhancement of prophylactic and therapeutic efficiency of administered enzyme. Compounds K117, K269, K075, and trimedoxime were found to be the most potent reactivators of inhibited butyrylcholinesterase. CONCLUSIONS: In this work, we have evaluated only reactivation of paraoxon-inhibited cholinesterases. To get better understanding of this problem, a larger number of organophosphorus inhibitors should be used.</P>
( Swarnjeet Singh ),( Kamil Kuca ),( Anu Kalia ) 한국균학회 2020 Mycobiology Vol.48 No.5
Use of nanoparticles (NPs) in several commercial products has led to emergence of novel contaminants of air, soil and water bodies. The NPs may exhibit greater ecotoxicity due to nano-scale dependent properties over their bulk counterparts. The present investigation explores the effect of in vitro supplementation of TiO<sub>2</sub>, silica and silver NPs on radial growth and ultrastructural changes in the hyphae and spores of two mushroom genera, Ganoderma lucidum and Volvariella volvaceae. A concentration dependent decrease in radial growth on NP amended potato dextrose agar medium was recorded. However, in comparison to control, there was decrease in radial diameter on supplementation with TiO<sub>2</sub> NPs while an increase was recorded for silica and silver NPs amendments as compared to their bulk salts at same concentrations after 48 h of incubation. Optical microscopy studies showed decrease in the number of spores while increase in spore diameter and thinning of hyphal diameter on NPs supplementation. Scanning electron microscopy analysis of fungal growth showed presence of deflated and oblong spores in two fruiting strains of Ganoderma while Volvariella exhibited decreased sporulation. Further, hyphal thinning and branching was recorded in response to NP amendments in both the test mushrooms. Enhancement of protein content was observed on NP compared to bulk supplementation for all cultures, concentrations and hours of incubation except for TiO<sub>2</sub> NPs. Likewise, bulk and NP supplementations (at 100mg L<sup>-1</sup>) resulted in enhanced laccase activity with occurrence of laccase specific protein bands on SDS-PAGE analysis.
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>
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.