Synthesis, Molecular Docking, and Bioactivity Study of Novel Hybrid Benzimidazole Urea Derivatives: A Promising α-Amylase and α-Glucosidase Inhibitor Candidate with Antioxidant Activity

A novel series of benzimidazole ureas were elaborated using 2-(1 -benzoimidazol-2-yl) aniline and the appropriate isocyanates . The antioxidant and possible antidiabetic activities of the target benzimidazole-ureas were evaluated. Almost all compounds displayed strong to moderate antioxidant activities. When tested using the three antioxidant techniques, TAC, FRAP, and MCA, compounds and exhibited marked activity. The most active antioxidant compound in this family was compound , which had excellent activity using four different methods: TAC, FRAP, DPPH-SA, and MCA. In vitro antidiabetic assays against α-amylase and α-glucosidase enzymes revealed that the majority of the compounds tested had good to moderate activity. The most favorable results were obtained with compounds , , and , and analysis revealed that compounds (IC = 18.65 ± 0.23 μM), (IC = 20.7 ± 0.06 μM), and (IC = 22.33 ± 0.12 μM) had good α-amylase inhibitory potential comparable to standard acarbose (IC = 14.21 ± 0.06 μM). Furthermore, the inhibitory effect of (IC = 17.47 ± 0.03 μM), (IC = 21.97 ± 0.19 μM), and (IC = 23.01 ± 0.12 μM) on α-glucosidase was also comparable to acarbose (IC = 15.41 ± 0.32 μM). According to in silico molecular docking studies, compounds had considerable affinity for the active sites of human lysosomal acid α-glucosidase (HLAG) and pancreatic α-amylase (HPA), indicating that the majority of the examined compounds had potential anti-hyperglycemic action.