Combined in vitro and in silico approach to define alangimarckine from Thunbergia mysorensis 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 T. mysorensis 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 in silico 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 in silico research to clarify the mechanism by which T. mysorensis 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 in vitro inhibition of α-glucosidase, which was efficient in comparison to both MeL and acarbose. Therefore, our research suggests that alangimarckine and MeL from T. mysorensis may function as potent antidiabetic medications. Alangimarckine could be used in in vivo and clinical investigations to specify its antidiabetic properties that target α-glucosidase inhibition.