Acetylcholinesterase-inhibiting activity of salicylanilide N-alkylcarbamates and their molecular docking.

ABSTRACT: 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'(₃,₄) 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 sli

SUBMITTER: Imramovsky A 

PROVIDER: S-EPMC6268027 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature