In Vitro Enzymatic and Kinetic Studies, and In Silico Drug-Receptor Interactions, and Drug-Like Profiling of the 5-Styrylbenzamide Derivatives as Potential Cholinesterase and β-Secretase Inhibitors with Antioxidant Properties
The 5-(styryl)anthranilamides were transformed into the corresponding 5-styryl-2-(<i>p</i>-tolylsulfonamido)benzamide derivatives. These 5-styrylbenzamide derivatives were evaluated through enzymatic assays in vitro for their capability to inhibit acetylcholinesterase (AChE), butyrylchol...
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| Main Authors: | , , , |
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| Format: | Book |
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MDPI AG,
2021-04-01T00:00:00Z.
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| Summary: | The 5-(styryl)anthranilamides were transformed into the corresponding 5-styryl-2-(<i>p</i>-tolylsulfonamido)benzamide derivatives. These 5-styrylbenzamide derivatives were evaluated through enzymatic assays in vitro for their capability to inhibit acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and β-secretase (BACE-1) activities as well as for antioxidant potential. An in vitro cell-based antioxidant activity assay involving lipopolysaccharides (LPS)-induced reactive oxygen species (ROS) production revealed that compounds <b>2a</b> and <b>3b</b> have the capability of scavenging free radicals. The potential of the most active compound, 5-styrylbenzamide (<b>2a</b>), to bind copper (II) or zinc (II) ions has also been evaluated spectrophotometrically. Kinetic studies of the most active derivatives from each series against the AChE, BChE, and β-secretase activities have been performed. The experimental results are complemented with molecular docking studies into the active sites of these enzymes to predict the hypothetical protein-ligand binding modes. Their drug likeness properties have also been predicted. |
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| Item Description: | 10.3390/antiox10050647 2076-3921 |