Ruellia tuberosa L. is a folk remedy in the treatment of diabetes mellitus. However, its hypoglycemic activity has not been investigated so far. In the present study, the antidiabetic mechanism of the n-hexane fraction of methanolic extract (HFME) of this plant was investigated in silico, in vitro, and in vivo. In silico study was performed using AutoDock4.2 software. In vitro α-amylase inhibitory activity was investigated by starch-iodine method. A single dose of 450 mg/kg HFME for 14 days was subjected to an antidiabetic screening in vivo by a multiple low dose streptozotocin (MLD-STZ) induced rats. Molecular modeling results show that Betulin exhibited noncompetitive α-amylase inhibitory activities. The effect of HFME elicited significant reductions of diabetic rat blood glucose. A single dose administration of HFME inhibited α-amylase activity in vivo (P < 0.01) compared to a diabetic control group. Moreover, this extract strongly inhibited the α-amylase activity in vitro (IC50 0.14 ± 0.005 mg/mL). It is concluded that HFME exerted an antidiabetic effect via α-amylase inhibitor. Our findings provide a possible hypoglycemic action of R. tuberosa L. as an alternative therapy in the management of diabetes.
To understand the structural features that dictate the selectivity of the two isoforms of the prostaglandin H2 synthase (PGHS/COX), the three-dimensional (3D) structure of COX-1/COX-2 was assessed by means of binding energy calculation of virtual molecular dynamic with using ligand alpha-Patchouli alcohol isomers. Molecular interaction studies with COX-1 and COX-2 were done using the molecular docking tools by Hex 8.0. Interactions were further visualized by using Discovery Studio Client 3.5 software tool. The binding energy of molecular interaction was calculated by AMBER12 and Virtual Molecular Dynamic 1.9.1 software. The analysis of the alpha-Patchouli alcohol isomer compounds showed that all alpha-Patchouli alcohol isomers were suggested as inhibitor of COX-1 and COX-2. Collectively, the scoring binding energy calculation (with PBSA Model Solvent) of alpha-Patchouli alcohol isomer compounds (CID442384, CID6432585, CID3080622, CID10955174, and CID56928117) was suggested as candidate for a selective COX-1 inhibitor and CID521903 as nonselective COX-1/COX-2.
Inhibition of α-amylase is an important strategy to control post-prandial hyperglycemia. The present study on Ruellia tuberosa, known as traditional anti-diabetic agent, is being provided in silico study to identify compounds inhibiting α-amylase in rat and human. Compounds were explored from PubChem database. Molecular docking was studied using the autodock4. The interactions were further visualized and analyzed using the Accelrys Discovery Studio version 3.5. Binding energy of compounds to α-amylase was varying between -1.92 to -6.66 kcal/mol in rat pancreatic alpha amylase and -3.06 to -8.42kcal/mol in human pancreatic alpha amylase, and inhibition konstanta (ki) was varying between 13.12- 39460µM in rat and 0.67-5600µM in human. The docking results verify that betulin is the most potential inhibitor of all towards rat model alpha amylase and human alpha amylase. Further analysis reveals that betulin could be a potential inhibitor with non-competitive pattern like betulinic acid. In comparison, betulin has smaller Ki (0.67µM) than acarbose (2.6 µM), which suggesting that betulin is more potential as inhibitor than acarbose, but this assumption must be verified in vitro.
