乳铁蛋白
化学
金属
纳米技术
计算生物学
材料科学
生物化学
生物
有机化学
作者
Paweł Fijałkowski,Paweł Pomastowski,Rudi van Eldik,Katarzyna Rafińska
标识
DOI:10.1016/j.ijbiomac.2025.146531
摘要
Lactoferrin (Lf) is a multifunctional glycoprotein of the transferrin family that plays a crucial role in iron metabolism, immune regulation, and antimicrobial defense. This review explores the structural properties and metal-binding mechanisms of lactoferrin, highlighting its interactions with various metal ions including manganese, silver, zinc, copper, bismuth, vanadium, and lanthanides. These interactions occur through specific coordination at traditional iron-binding sites as well as via nonspecific surface interactions and redox-based mechanisms. This review provides a comprehensive analysis of lactoferrin's structural properties, biological sources and metal-binding mechanisms. The binding of metal ions significantly influences lactoferrin's biochemical activity, affecting its antimicrobial, antiviral, prebiotic, and immunomodulatory properties. The emerging evidence on lactoferrin's interactions with bioactive metal ions indicate its relevance in dairy science, nutrition, and biomedical applications. Understanding these interactions provides new insights into the development of dairy-derived functional foods, pharmaceuticals or sensors.
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