values at the nanomolar level. Enantioselective analyses showed that S-enantiomers were significantly more effective in AChE inhibition, while enzyme-specific inverse stereoselective preferences emerged in BChE inhibition. Experimental findings were supported by induced coherent molecular docking (IFD), MM-GBSA binding free energy calculations, and 250-ns molecular dynamics simulations. In silico analyses confirmed that 7b exhibited high stability and strong interactions in the AChE active site and 7a in the BChE active pocket. Furthermore, ADME analyses revealed that the compounds possessed favorable pharmacokinetic and drug-like properties. In conclusion, this study demonstrates that chiral anthranilic diamide derivatives are promising novel AChE/BChE inhibitor candidates that act as potent and selective cholinesterase inhibitors.
Tunç et al. (Fri,) studied this question.