Benzenesulfonamide derivatives as potent acetylcholinesterase, α-glycosidase, and glutathione S-transferase inhibitors: biological evaluation and molecular docking studies.

Sulfonamide derivatives exhibit a wide biological activity and can function as potential medical molecules in the development of a drug. Studies have reported that the compounds have an effect on many enzymes. In this study, the derivatives of amine sulfonamide (-) were prepared with reduced imine compounds (-) with NaBH in methanol. The synthesized compounds were fully characterized by spectral data and analytical. The effect of the synthesized derivatives on acetylcholinesterase (AChE), glutathione S-transferase (GST) and α-glycosidase (α-GLY) enzymes were determined. For the AChE and α-GLY, the most powerful inhibition was observed on and series with value in the range 2.26 ± 0.45-3.57 ± 0.97 and 95.73 ± 13.67-102.45 ± 11.72 µM, respectively. values of the series for GST were found in the range of 22.76 ± 1.23-49.29 ± 4.49. Finally, the compounds have a stronger inhibitor in lower concentrations by the attachment of functional electronegative groups such as two halogens (-Br and -CI), -OH to the benzene ring and -SONH. The crystal structures of AChE, α-GLY, and GST in complex with selected derivatives and show the importance of the functional moieties in the binding modes within the receptors.Communicated by Ramaswamy H. Sarma.