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Design; synthesis and biological evaluation of tacrine-sulphonamide hybrids as a potent acetylcholinesterase inhibitor
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DOI：10.1039/D6RA00900J.png)
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Abstract
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Novel tacrine-based sulphonamide derivatives were designed and evaluated for their ability to inhibit acetylcholinesterase (AChE) using molecular docking and in vitro assays. Docking studies revealed strong interactions with key active-site residues; including Trp86; Trp286; Tyr337; and Phe338; mediated through π–π stacking; π-cation interactions; hydrogen bonding; and hydrophobic contacts. Among the synthesized compounds; 6g; 6i; 6j; and 6k exhibited superior binding affinities; with compound 6j demonstrating the highest docking score of −9.18 kcal mol−1 and a binding energy of −97.92 kcal mol−1. In vitro screening using Ellman's method confirmed potent AChE inhibition; with IC50 values in the nanomolar range. Structure–activity relationship analysis indicated that methyl-substituted piperidine derivatives significantly enhanced inhibitory potency; with compounds 6j and 6k achieving IC50 values of 7.40 nM and 11.33 nM; respectively.
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