Mechanism of inhibition of alpha-amylase by caffeic acid using in-vitro and in-silico techniques.

Type-two diabetes, characterised by insulin resistance or inadequate insulin production, is prevalent among adults. The α-amylase enzyme contributes to carbohydrate digestion, elevating postprandial glucose levels. Natural compounds like caffeic acid offer a solution. This study investigates α-amylase inhibition in-vitro and in-silico methods, emphasising the connection between phenolic compounds and antidiabetic efficacy for in-silico analysis. Enzyme kinetics, IC, and molecular docking examine caffeic acid's inhibitory action on α-amylase, comparing it with gallic acid and acarbose. Caffeic acid outperforms acarbose with an IC of 4.505 mg/mL versus 16.81 mg/mL, showcasing strong antidiabetic activity. Caffeic acid's superior 1,1-diphenyl-2-picrylhydrazyl (DPPH) inhibition (90.67%) compared to gallic acid (55.76%) indicates potent antioxidative and antidiabetic properties. Molecular docking reveals hydrogen bonding between caffeic acid and α-amylase. These insights lay the groundwork for phenolic-based diabetic therapies, offering less expensive treatment for diabetes patients.