Kinetic Studies, Antioxidant Activities, Enzyme Inhibition Properties and Molecular Docking of 1,3-Dihydro Derivatives

Abstract

The acid catalyzed hydrolysis of the N-(p-substitutedphenyl) phthalimides in three different acids was investigated at 50.0 +/- 0.1 degrees C. Two different antioxidant activity tests as DPPH center dot and ABTS(center dot+) scavenging activities, and three various enzyme inhibition activity tests as urease, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) inhibition activities, were applied. Compound 3c (2.03 mu g/mL) has higher antioxidant activity than other compounds and standards according to DPPH test. In AChE assay, compounds 3a and 3b (13.13 and 9.59 mu g/mL) has higher enzyme inhibition activity than the standard Galantamine (14.37 mu g/mL). In BChE and urease tests, all compounds (6.84-13.60 and 10.49-17.73 mu g/mL) have higher enzyme inhibition activity than the standard Galantamine (49.40 mu g/mL) and thiourea (26.19 mu g/mL), respectively. The molecule interaction for each of the three compounds with the active sites of AChE, BChE, and urease enzymes was examined via molecular docking simulations.