Combined <i>in vitro</i> and <i>in silico</i> approach to define alangimarckine from <i>Thunbergia mysorensis</i> leaves as a potential inhibitor of α-glucosidase

The current work investigated biocomputational methodologies for α-glucosidase inhibition to examine the antidiabetic potential of methanolic extract of <i>T. mysorensis</i> leaves (MeL). MeL intensely impeded yeast-glucosidase, which is vital for treating postprandial hyperglycemia (IC₅₀ = 5.76 ± 0.10 μg/mL) in comparison to an acarbose control (IC₅₀ = 7.98 ± 0.23 μg/mL). The MeL is affected by phytochemical profiling employing LC-MS, GC-MS, and HPLC analysis to determine the bioactive components responsible for the antidiabetic activity. The specified phytocompounds were employed <i>in silico</i> research following the bioactive profiling, where they were docked into the inhibitor binding site of α-glucosidase. Molecular docking simulations, molecular dynamics simulations, and binding free energy inquiries were utilized <i>in silico</i> research to clarify the mechanism by which <i>T. mysorensis</i> phytocompounds block α-glucosidase. Alangimarckine is a glucocorticoid that is used to treat nasal symptoms. Alangimarckine inhibited the target enzyme with greater binding efficiency (-9.7 kcal/mol) than the acarbose control (-8.6 kcal/mol) during molecular docking. Concerning molecular dynamics simulation studies, Alangimarckine-α-glucosidase complex was found to be stable inside the inhibitor binding site of the protein, compared to the acarbose -α-glucosidase complex. Additionally, alangimarckine inhibited α-glucosidase at IC₅₀ = 5.32 ± 0.19 μg/mL during <i>in vitro</i> inhibition of α-glucosidase, which was efficient in comparison to both MeL and acarbose. Therefore, our research suggests that alangimarckine and MeL from <i>T. mysorensis</i> may function as potent antidiabetic medications. Alangimarckine could be used in <i>in vivo</i> and clinical investigations to specify its antidiabetic properties that target α-glucosidase inhibition.