LAUSR

This study was designed to screen novel thiourea derivatives against different enzymes, such as α‐amylase, α‐glucosidase, protein tyrosine phosphatase 1 B, and advanced glycated end product (AGEs). A cytotoxicity analysis was performed using rat L6 myotubes and molecular docking analysis was performed to map the binding interactions between the active compounds and α‐amylase and α‐glucosidase. The data revealed the potency of five compounds, including E (1‐(2,4‐difluorophenyl)‐3‐(3,4‐dimethyl phenyl) thiourea), AG (1‐(2‐methoxy‐5‐(trifluoromethyl) phenyl)‐3‐(3‐methoxy phenyl) thiourea), AF (1‐(2,4‐dichlorophenyl)‐3‐(4‐ethylphenyl) thiourea), AD (1‐(2,4‐dichlorophenyl)‐3‐(4‐ethylphenyl) thiourea), and AH (1‐(2,4‐difluorophenyl)‐3‐(2‐iodophenyl) thiourea), showed activity against α‐amylase. The corresponding percentage inhibitions were found to be 85 ± 1.9, 82 ± 0.7, 75 ± 1.2, 72 ± 0.4, and 65 ± 1.1%, respectively. These compounds were then screened using in vitro assays. Among them, AH showed the highest activity against α‐glucosidase, AGEs, and PTP1B, with percentage inhibitions of 86 ± 0.4% (IC50 = 47.9 μM), 85 ± 0.7% (IC50 = 49.51 μM), and 85 ± 0.5% (IC50 = 79.74 μM), respectively. Compound AH showed an increased glucose uptake at a concentration of 100 μM. Finally, an in vivo study was conducted using a streptozotocin‐induced diabetic mouse model and PTP1B expression was assessed using real‐time PCR. Additionally, we examined the hypoglycemic effect of compound AH in diabetic rats compared to the standard drug glibenclamide.