Antidiabetic Activity of Ruellia tuberosa L., Role of α-Amylase Inhibitor: In Silico, In Vitro, and In Vivo Approaches

Table 4

In silico study results.

Ligand name/PubChem ID	Substrate	Target molecule; (PDB ID)	EI complex; (µM)	of EI complex; (kcal/mol)	Docking score; (3)	Predicted inhibition mode	Inhibition mode in the previous study	Reference	H-bond interaction	Graphical image of ligand-molecule complex
Betulin/CID 72326	Maltose	Rattus alpha amylase model	13.66	−6.66	23.36 µM 29.99 µM	Noncompetitive	—	—	ASN374, ASN374, ASN376
Betulinic acid/CID 64971	Maltose	Porcine pancreatic α-amylase (1.ose)	75.66	−5.62	149.13 µM ≈ 144.26 µM	Noncompetitive	Non; competitive	Karthic et al. [14]	—
Bisdemethoxycurcumin/; CID 5315472	Maltose	Human alpha amylase (3.old)	45.86	−5.92	83.49 µM ≠ 39.55 µM	Un; competitive or competitive	Un; competitive	Najafian [15]	ARG389
Curcumin/CID 969516	Maltose	Human alpha amylase (3.old)	260.62	−4.89	841.04 µM ≠ 0.044 µM	Un; competitive or competitive	Competitive	Karthic et al. [14]	LYS 200, GLY 306, HIS 201

Graphical image showed interaction between ligand-substrate and enzyme complexes. Yellow color is ligand, black color is substrate, and whole structure is of amylase.