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Statements

Subject Item
n2:RIV%2F00179906%3A_____%2F13%3A10159246%21RIV14-MZ0-00179906
rdf:type
n13:Vysledek skos:Concept
rdfs:seeAlso
http://www.mdpi.com/1422-0067/14/8/16076
dcterms:description
Acetylcholinesterase (AChE) reactivators (oximes) are compounds predominantly targeting the active site of the enzyme. Toxic effects of organophosphates nerve agents (OPNAs) are primarily related to their covalent binding to AChE and butyrylcholinesterase (BChE), critical detoxification enzymes in the blood and in the central nervous system (CNS). After exposure to OPNAs, accumulation of acetylcholine (ACh) overstimulates receptors and blocks neuromuscular junction transmission resulting in CNS toxicity. Current efforts at treatments for OPNA exposure are focused on non-quaternary reactivators, monoisonitrosoacetone oximes (MINA), and diacylmonoxime reactivators (DAM). However, so far only quaternary oximes have been approved for use in cases of OPNA intoxication. Five acetylcholinesterase reactivator candidates (K027, K075, K127, K203, K282) are presented here, together with pharmacokinetic data (plasma concentration, human serum albumin binding potency). Pharmacokinetic curves based on intramuscular application of the tested compounds are given, with binding information and an evaluation of structural relationships. Human Serum Albumin (HSA) binding studies have not yet been performed on any acetylcholinesterase reactivators, and correlations between structure, concentration curves and binding are vital for further development. HSA bindings of the tested compounds were 1% (HI-6), 7% (obidoxime), 6% (trimedoxime), and 5%, 10%, 4%, 15%, and 12% for K027, K075, K127, K203, and K282, respectively. Acetylcholinesterase (AChE) reactivators (oximes) are compounds predominantly targeting the active site of the enzyme. Toxic effects of organophosphates nerve agents (OPNAs) are primarily related to their covalent binding to AChE and butyrylcholinesterase (BChE), critical detoxification enzymes in the blood and in the central nervous system (CNS). After exposure to OPNAs, accumulation of acetylcholine (ACh) overstimulates receptors and blocks neuromuscular junction transmission resulting in CNS toxicity. Current efforts at treatments for OPNA exposure are focused on non-quaternary reactivators, monoisonitrosoacetone oximes (MINA), and diacylmonoxime reactivators (DAM). However, so far only quaternary oximes have been approved for use in cases of OPNA intoxication. Five acetylcholinesterase reactivator candidates (K027, K075, K127, K203, K282) are presented here, together with pharmacokinetic data (plasma concentration, human serum albumin binding potency). Pharmacokinetic curves based on intramuscular application of the tested compounds are given, with binding information and an evaluation of structural relationships. Human Serum Albumin (HSA) binding studies have not yet been performed on any acetylcholinesterase reactivators, and correlations between structure, concentration curves and binding are vital for further development. HSA bindings of the tested compounds were 1% (HI-6), 7% (obidoxime), 6% (trimedoxime), and 5%, 10%, 4%, 15%, and 12% for K027, K075, K127, K203, and K282, respectively.
dcterms:title
Acetylcholinesterase reactivators (HI-6, obidoxime, trimedoxime, K027, K075, K127, K203, K282): structural evaluation of human serum albumin binding and absorption Kinetics Acetylcholinesterase reactivators (HI-6, obidoxime, trimedoxime, K027, K075, K127, K203, K282): structural evaluation of human serum albumin binding and absorption Kinetics
skos:prefLabel
Acetylcholinesterase reactivators (HI-6, obidoxime, trimedoxime, K027, K075, K127, K203, K282): structural evaluation of human serum albumin binding and absorption Kinetics Acetylcholinesterase reactivators (HI-6, obidoxime, trimedoxime, K027, K075, K127, K203, K282): structural evaluation of human serum albumin binding and absorption Kinetics
skos:notation
RIV/00179906:_____/13:10159246!RIV14-MZ0-00179906
n13:predkladatel
n14:ico%3A00179906
n3:aktivita
n16:I
n3:aktivity
I
n3:cisloPeriodika
8
n3:dodaniDat
n7:2014
n3:domaciTvurceVysledku
n19:6306888
n3:druhVysledku
n17:J
n3:duvernostUdaju
n4:S
n3:entitaPredkladatele
n15:predkladatel
n3:idSjednocenehoVysledku
59335
n3:idVysledku
RIV/00179906:_____/13:10159246
n3:jazykVysledku
n12:eng
n3:klicovaSlova
nerve agent; antidote; reactivator; pharmacokinetics; human serum albumin; oximes; acetylcholinesterase
n3:klicoveSlovo
n6:nerve%20agent n6:human%20serum%20albumin n6:antidote n6:reactivator n6:acetylcholinesterase n6:pharmacokinetics n6:oximes
n3:kodStatuVydavatele
CH - Švýcarská konfederace
n3:kontrolniKodProRIV
[FEDDD98E2615]
n3:nazevZdroje
International Journal of Molecular Sciences
n3:obor
n8:FR
n3:pocetDomacichTvurcuVysledku
1
n3:pocetTvurcuVysledku
4
n3:rokUplatneniVysledku
n7:2013
n3:svazekPeriodika
14
n3:tvurceVysledku
Žďárová Karasová, Jana Kuča, Kamil Zemek, Filip Šepsová, Vendula
n3:wos
000328501300045
s:issn
1422-0067
s:numberOfPages
11
n18:doi
10.3390/ijms140816076