About: Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
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. (en)
Title	Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking (en)
skos:prefLabel	Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking (en)
skos:notation	RIV/62157124:16370/12:43871097!RIV13-MSM-16370___
http://linked.open...avai/predkladatel	Farmaceutická fakulta
http://linked.open...avai/riv/aktivita	I S
http://linked.open...avai/riv/aktivity	I, S
http://linked.open...iv/cisloPeriodika	9
http://linked.open...vai/riv/dodaniDat	2013
http://linked.open...aciTvurceVysledku	Vančo, Ján Jampílek, Josef
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Veterinární a farmaceutická univerzita Brno / Farmaceutická fakulta
http://linked.open...dnocenehoVysledku	120896
http://linked.open...ai/riv/idVysledku	RIV/62157124:16370/12:43871097
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	molecular docking; lipophilicity; in vitro acetylcholinesterase inhibition; 4-chloro-2-(chlorophenylcarbamoyl)phenyl alkylcarbamates (en)
http://linked.open.../riv/klicoveSlovo	4-chloro-2-(chlorophenylcarbamoyl)phenyl alkylcarbamates molecular docking in vitro acetylcholinesterase inhibition lipophilicity
http://linked.open...odStatuVydavatele	CH - Švýcarská konfederace
http://linked.open...ontrolniKodProRIV	[2EBFC7266A9F]
http://linked.open...i/riv/nazevZdroje	Molecules
http://linked.open...in/vavai/riv/obor	FR
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	7 (xsd:int)
http://linked.open...UplatneniVysledku	2012
http://linked.open...v/svazekPeriodika	17
http://linked.open...iv/tvurceVysledku	Jampílek, Josef Vinšová, Jarmila Imramovský, Aleš Vančo, Ján Pauk, Karel Štěpánková, Šárka Monreal-Ferriz, Juana
http://linked.open...ain/vavai/riv/wos	000309269700013
issn	1420-3049
number of pages	17 (xsd:int)
http://bibframe.org/vocab/doi	10.3390/molecules170910142
http://localhost/t...ganizacniJednotka	16370
is http://linked.open...avai/riv/vysledek of	Acetylcholinesterase-Inhibiting Activity of Salicylanilide N-Alkylcarbamates and Their Molecular Docking

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 41 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software