Figure 6.

Molecular docking of the main three phenolic compounds and acarbose with α-amylase. The 3D docking structures of three phenolic compounds and acarbose were inserted into the hydrophobic cavity of α-amylase (blue): gallic acid (A1); ellagic acid (B1); procyanidin C3 (C1); acarbose (D1). The conformations of active molecules interactions with amino acid residues in the active site of α-amylase: gallic acid (A2), ellagic acid (B2), procyanidin C3 (C2), and acarbose (D2) with residues in the active sites of the α-amylase, respectively. The dashed line stands for hydrogen bonds.