Login for students

Login for employees

Publication detail

Novel Cholinesterases Inhibitors Based on O-Aromatic N,N-Disubstituted Carbamates and Thiocarbamates
Authors: Krátký Martin | Štěpánková Šárka | Vorčáková Katarína | Švarcová Markéta | Vinšová Jarmila
Year: 2016
Type of publication: článek v odborném periodiku
Name of source: Molecules
Page from-to: "191-1"-"191-10"
Titles:
Language Name Abstract Keywords
cze Nové cholinesterázové inhibitory na bázi karbamátů a thiokarbamátů Pomocí Ellmanovy metody byla sledována schopnost 20 nových salicylanilidových karbamátů a thiokarbamátů inhibovat acetylcholinesterázu a butyrylcholinesterázu. karbamáty, cholinesterázy
eng Novel Cholinesterases Inhibitors Based on O-Aromatic N,N-Disubstituted Carbamates and Thiocarbamates Based on the presence of carbamoyl moiety, twenty salicylanilide N,N-disubstituted (thio)carbamates were investigated using Ellman’s method for their ability to inhibit acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). O-Aromatic (thio)carbamates exhibited weak to moderate inhibition of both cholinesterases with IC50 values within the range of 1.60 to 311.0 μM. IC50 values for BChE were mostly lower than those obtained for AChE; four derivatives showed distinct selectivity for BChE. All of the (thio)carbamates produced a stronger inhibition of AChE than rivastigmine, and five of them inhibited BChE more effectively than both established drugs rivastigmine and galantamine. In general, 5-chloro-2-hydroxy-N-[4-(trifluoromethyl)- phenyl]benzamide, 2-hydroxy-N-phenylbenzamide as well as N-methyl-N-phenyl carbamate derivatives led to the more potent inhibition. O-{4-Chloro-2-[(4-chlorophenyl)carbamoyl]phenyl} dimethylcarbamothioate was identified as the most effective AChE inhibitor (IC50 = 38.98 μM), while 2-(phenylcarbamoyl)phenyl diphenylcarbamate produced the lowest IC50 value for BChE (1.60 μM). Results from molecular docking studies suggest that carbamate compounds, especially N,Ndiphenyl substituted representatives with considerable portion of aromatic moieties may work as non-covalent inhibitors displaying many interactions at peripheral anionic sites of both enzymes. Mild cytotoxicity for HepG2 cells and consequent satisfactory calculated selectivity indexes qualify several derivatives for further optimization. acetylcholinesterase; butyrylcholinesterase; carbamate; enzyme inhibition; salicylanilide; thiocarbamate

Departments

Other Parts

Map

en.mapy.cz

Services

Popular Links

© 2023 University of Pardubice, Studentská 95, 532 10 Pardubice 2
Phone: +420 466 036 111, 466 036 112, 466 036 113
Webmaster, RSS
Data box ID: f5vj9hu
Accessibility Statement
CC BY-NC-ND 4.0Creative CommonsAttributionNonCommercialNoDerivatives