Computer Simulation of Molecular Docking of α-Lactalbumin with Saponins

Small molecule saponins are highly physiologically active and exert their biological effects only when interacting with biomolecules in the target cells in the human body. α-Lactalbumin (α-LA) is a globular protein that binds to hydrophobic ligands and has been used as a functional ingredient in the food industry. In this study, the interaction between two types of saponins (dammarane-type and oleanane-type) and α-LA was investigated using computer simulations, and their interaction patterns were imaged. The molecular docking results showed that each type of saponins binds to amino acid residues within the active pocket of α-LA via hydrophobic interactions and hydrogen bonding. However, dammarane-type saponins are more complex in structure, providing more binding sites, and they form hydrogen bonds via greater force.