Abstract: 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.

Key words: dammarane-type saponins; oleanane-type saponins; α-lactalbumin; molecular docking; interaction

摘要： 皂苷小分子具有很强的生理活性，在人体中必须与靶细胞生物大分子相互作用才能发挥其生物作用。α-乳 白蛋白（α-lactalbumin，α-LA）是球状蛋白质，能结合疏水配体，在食品工业作为功能性配料。采用计算机模拟的 方法，对2 类皂苷（达玛烷型皂苷和齐墩果型皂苷）和α-LA相互作用进行研究，并获得其相互作用模式的相关图 像。分子对接结果表明，2 种类型的皂苷与α-LA活性口袋内的氨基酸残基均以疏水相互作用及氢键作用结合，但达 玛烷型皂苷结构更复杂，可以提供更多结合位点，且其形成氢键的作用力更强。

关键词: 达玛烷型皂苷；齐墩果型皂苷；α-乳白蛋白；分子对接；相互作用