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Statements

Subject Item
n2:RIV%2F62157124%3A16370%2F12%3A43871097%21RIV13-MSM-16370___
rdf:type
n7:Vysledek skos:Concept
dcterms:description
A series of twenty-five novel salicylanilide N-alkylcarbamates were investigated as potential acetylcholinesterase inhibitors. The compounds were tested for their ability to inhibit acetylcholinesterase (AChE) from electric eel (Electrophorus electricus L.). Experimental lipophilicity was determined, and the structure-activity relationships are discussed. The mode of binding in the active site of AChE was investigated by molecular docking. All the discussed compounds expressed significantly higher AChE inhibitory activity than rivastigmine and slightly lower than galanthamine. Disubstitution by chlorine in C-(3,C-4)' of the aniline ring and the optimal length of hexyl-undecyl alkyl chains in the carbamate moiety provided the most active AChE inhibitors. Monochlorination in C-(4)' exhibited slightly more effective AChE inhibitors than in C-(3)'. Generally it can be stated that compounds with higher lipophilicity showed higher inhibition, and the activity of the compounds is strongly dependent on the length of the N-alkyl chain. A series of twenty-five novel salicylanilide N-alkylcarbamates were investigated as potential acetylcholinesterase inhibitors. The compounds were tested for their ability to inhibit acetylcholinesterase (AChE) from electric eel (Electrophorus electricus L.). Experimental lipophilicity was determined, and the structure-activity relationships are discussed. The mode of binding in the active site of AChE was investigated by molecular docking. All the discussed compounds expressed significantly higher AChE inhibitory activity than rivastigmine and slightly lower than galanthamine. Disubstitution by chlorine in C-(3,C-4)' of the aniline ring and the optimal length of hexyl-undecyl alkyl chains in the carbamate moiety provided the most active AChE inhibitors. Monochlorination in C-(4)' exhibited slightly more effective AChE inhibitors than in C-(3)'. Generally it can be stated that compounds with higher lipophilicity showed higher inhibition, and the activity of the compounds is strongly dependent on the length of the N-alkyl chain.
dcterms:title
Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking
skos:prefLabel
Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking
skos:notation
RIV/62157124:16370/12:43871097!RIV13-MSM-16370___
n7:predkladatel
n8:orjk%3A16370
n3:aktivita
n15:I n15:S
n3:aktivity
I, S
n3:cisloPeriodika
9
n3:dodaniDat
n13:2013
n3:domaciTvurceVysledku
n11:4192478 n11:9033793
n3:druhVysledku
n18:J
n3:duvernostUdaju
n12:S
n3:entitaPredkladatele
n4:predkladatel
n3:idSjednocenehoVysledku
120896
n3:idVysledku
RIV/62157124:16370/12:43871097
n3:jazykVysledku
n17:eng
n3:klicovaSlova
molecular docking; lipophilicity; in vitro acetylcholinesterase inhibition; 4-chloro-2-(chlorophenylcarbamoyl)phenyl alkylcarbamates
n3:klicoveSlovo
n9:4-chloro-2-%28chlorophenylcarbamoyl%29phenyl%20alkylcarbamates n9:molecular%20docking n9:in%20vitro%20acetylcholinesterase%20inhibition n9:lipophilicity
n3:kodStatuVydavatele
CH - Švýcarská konfederace
n3:kontrolniKodProRIV
[2EBFC7266A9F]
n3:nazevZdroje
Molecules
n3:obor
n14:FR
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
7
n3:rokUplatneniVysledku
n13:2012
n3:svazekPeriodika
17
n3:tvurceVysledku
Štěpánková, Šárka Vančo, Ján Monreal-Ferriz, Juana Pauk, Karel Jampílek, Josef Vinšová, Jarmila Imramovský, Aleš
n3:wos
000309269700013
s:issn
1420-3049
s:numberOfPages
17
n16:doi
10.3390/molecules170910142
n19:organizacniJednotka
16370