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- W4200450215 endingPage "103645" @default.
- W4200450215 startingPage "103645" @default.
- W4200450215 abstract "The alkyl and aryl derivatives of aniline are important starting materials in fine organic synthesis. Allyl bromide and benzyl chloride were taken as substrates for the alkylation reaction and as a halide ion scavenger. Triethylamine was utilized at reflux condition of N,N-dimethylacetamide (DMA). Novel synthesized N-benzyl and N-allyl aniline derivatives (1a-f) were evaluated to be highly potent inhibitors for acetylcholinesterase (AChE) and carbonic anhydrases (hCAs). The half maximal inhibitory concentration (IC50) of N-benzyl- and N-allyl aniline derivatives were calculated between 243.11 and 633.54 nM for hCA I, 296.32–518.37 nM for hCA II and 182.45–520.21 nM for AChE enzymes. On the other hand, Ki values are in the range of 149.24 ± 15.59 to 519.59 ± 102.27 nM for AChE, 202.12 ± 16.21 to 635.31 ± 45.33 nM for hCA I and 298.57 ± 94.13 to 511.18 ± 115.98 nM for hCA II isoenzyme. Additionally, in silico molecular docking computations were performed with Autodock Vina program to support the experimental in vitro studies for both hCAs and AChE inhibitors. The in silico molecular docking results demonstrated that the scores are in good agreement with the experimental results." @default.
- W4200450215 created "2021-12-31" @default.
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- W4200450215 creator A5088168451 @default.
- W4200450215 date "2022-03-01" @default.
- W4200450215 modified "2023-10-17" @default.
- W4200450215 title "Synthesis and inhibition profiles of N-benzyl- and N-allyl aniline derivatives against carbonic anhydrase and acetylcholinesterase – A molecular docking study" @default.
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- W4200450215 doi "https://doi.org/10.1016/j.arabjc.2021.103645" @default.
- W4200450215 hasPublicationYear "2022" @default.
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