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
Creators: name: Kokila, N.R.
name: Mahesh, B.
name: Ramu, Ramith
name: Divakara, S.G.
name: Mruthunjaya, K.
name: Raghav, Neera
name: Shivanandappa, Thippeswamy Boreddy
Publisher: name: Taylor & Francis
Year: 2025
Subjects: subject: Biochemistry
subject: Space Science
subject: Medicine
subject: Cell Biology
subject: Genetics
subject: FOS: Biological sciences
subject: Molecular Biology
subject: Pharmacology
subject: Biotechnology
subject: Chemical Sciences not elsewhere classified
subject: Immunology
subject: FOS: Clinical medicine
subject: Biological Sciences not elsewhere classified
subject: Cancer

description: 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 (IC<sub>50</sub> = 5.76 ± 0.10 μg/mL) in comparison to an acarbose control (IC<sub>50</sub> = 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 IC<sub>50</sub> = 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. Antidiabetic potential of methanolic extract of <i>Thunbergia mysorensis</i> leaves was investigated.Phytochemical profiling of <i>T. mysorensis</i> was done using LCMS, GCMS, and HPLC analysis.The phytocompounds were subjected to <i>in silico</i> studies to check for α-glucosidase inhibition through molecular docking, dynamics simulation, and free energy calculations.Alangimarckine isolated was found to inhibit α-glucosidase with higher binding efficiency than acarbose (control) Antidiabetic potential of methanolic extract of <i>Thunbergia mysorensis</i> leaves was investigated. Phytochemical profiling of <i>T. mysorensis</i> was done using LCMS, GCMS, and HPLC analysis. The phytocompounds were subjected to <i>in silico</i> studies to check for α-glucosidase inhibition through molecular docking, dynamics simulation, and free energy calculations. Alangimarckine isolated was found to inhibit α-glucosidase with higher binding efficiency than acarbose (control)