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A novel series of benzimidazole ureas <b>3a–h</b> were elaborated using 2-(1<i>H</i>-benzoimidazol-2-yl) aniline <b>1</b> and the appropriate isocyanates <b>2a–h</b>. The antioxidant and possible antidiabetic activities of the target benzimidazole-ureas <b>3a–h</b> were evaluated. Almost all compounds <b>3a–h</b> displayed strong to moderate antioxidant activities. When tested using the three antioxidant techniques, TAC, FRAP, and MCA, compounds <b>3b</b> and <b>3c</b> exhibited marked activity. The most active antioxidant compound in this family was compound <b>3g</b>, 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 <b>3c</b>, <b>3e</b>, and <b>3g</b>, and analysis revealed that compounds <b>3c</b> (IC₅₀ = 18.65 ± 0.23 μM), <b>3e</b> (IC₅₀ = 20.7 ± 0.06 μM), and <b>3g</b> (IC₅₀ = 22.33 ± 0.12 μM) had good α-amylase inhibitory potential comparable to standard acarbose (IC₅₀ = 14.21 ± 0.06 μM). Furthermore, the inhibitory effect of <b>3c</b> (IC₅₀ = 17.47 ± 0.03 μM), <b>3e</b> (IC₅₀ = 21.97 ± 0.19 μM), and <b>3g</b> (IC₅₀ = 23.01 ± 0.12 μM) on α-glucosidase was also comparable to acarbose (IC₅₀ = 15.41 ± 0.32 μM). According to in silico molecular docking studies, compounds <b>3a–h</b> 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.