Article antidiabetic potential of peanut oil: inhibiting α-amylase and α-glucosidase using identified phytochemicals through in vitro and in silico studies

Background: Peanut oil is recognized for its mild flavor, high phytochemical content, medicinal potential, and other health advantages. Objective: This study, for the first time, evaluates the antidiabetic potential of peanut oil, known for its high phytochemical content and medicinal properties. Methods: The oil, collected from the El Oued region of Algeria, was extracted using the Soxhlet technique with n-hexane as the solvent. The obtained oil was subjected to gas chromatography–mass spectrometry (GC/MS) analysis. The antidiabetic effect in vitro was examined by inhibiting α-amylase and α-glucosidase enzymes. The molecular docking was performed using Molecular Operating Environment (MOE) software to assess the inhibitory potential of 20 identified phytochemical compounds against α-amylase (PDB ID: 2QV4) and α-glucosidase (PDB ID: 5NN8). Results: The oil is showing an inhibitory activity against α-amylase and α-glucosidase. Twenty fatty acid compounds representing 99.9% of the oil content were classified by gas chromatography–mass spectrometry (GC/MS) analysis into saturated fatty acids (SFA), monounsaturated fatty acids (MUFA), and polyunsaturated fatty acids (PUFA). Peanut oil demonstrated significant α-amylase inhibitory activity with an IC₅₀ value of 228.23 ± 5.68 μg/mL, surpassing the standard inhibitor, acarbose, which had an IC₅₀ of 3650.93 ± 10.70 μg/mL. Conversely, the α-glucosidase inhibition by peanut oil was less pronounced, with an IC₅₀ value exceeding 1,000 μg/mL. Acarbose exhibited a much stronger effect with an IC₅₀ of 405.77 ± 34.83 μg/mL. The molecular docking outcomes stated that stearic acid had a binding energy of −7.5729 kcal/mol and formed hydrogen bonds with residues like Gly164, Asn105, and Ala106, along with hydrophobic interactions with His201, Leu162, Tyr62, Leu165, and Trp59 in α-amylase inhibitory while in α-glusosidase inhibitory apt, the data revealed that compounds such as oxiraneoctanoic acid, 3-octyl, exhibited a favorable binding energy of −6.5120 kcal/mol and formed hydrogen bonds with key residues His674 and Asp616. Conclusion: These findings suggest that while peanut oil holds promise as a natural α-amylase inhibitor, its effect on α-glucosidase is relatively modest compared to the synthetic standard. Further research is recommended to explore the potential synergistic effects of peanut oil’s components for enhanced enzyme inhibition.