Chronic diseases, including cardiovascular and neurodegenerative diseases and cancer, are significant global health challenges. Oxidative stress, characterized by an imbalance between reactive oxygen species (ROS) production and antioxidant defenses, is a critical factor in the progression of these pathologies. Lactoferrin (Lf), a multifunctional iron-binding glycoprotein, has emerged as a promising therapeutic agent due to its potent antioxidant, anti-inflammatory, and iron-regulating properties. Lf plays a pivotal role in iron homeostasis by chelating iron, modulating its cellular uptake, and reducing ROS production, thereby mitigating oxidative stress-related tissue damage. Lf also demonstrates neuroprotective potential in diseases like Parkinson’s and Alzheimer’s, where it alleviates oxidative damage, regulates iron metabolism, and enhances antioxidant defenses. Furthermore, its ability to enhance endogenous antioxidant mechanisms, such as superoxide dismutase and glutathione peroxidase, underscores its systemic protective effects. Lf’s anti-inflammatory and antimicrobial activities also contribute to its broad-spectrum protective role in chronic diseases. This review consolidates evidence of Lf’s mechanisms in mitigating oxidative stress and highlights its therapeutic potential as a versatile molecule for preventing and managing chronic conditions linked to oxidative damage.

Human Lactoferrin (hLf), a multifunctional glycoprotein, has been analyzed through molecular docking to evaluate its role in apoptosis regulation and its potential as an anticancer agent. The docking results highlight XIAP (X-linked Inhibitor of Apoptosis Protein) and Caspase-3 as the most reliable targets, where hLf disrupts XIAP’s inhibition of Caspase-3 and Caspase-9, potentially restoring apoptotic signaling; hLf also stabilizes Caspase-3, enhancing its activation in intrinsic and extrinsic pathways. Weaker interactions were observed with Fas, Bcl-2, and Akt. hLf’s role in Fas signaling is likely due to expression upregulation rather than direct binding. In contrast, its binding to Bcl-2 may disrupt anti-apoptotic function, and its interaction with Akt suggests interference with pro-survival signaling. These findings suggest that hLf may promote apoptosis by enhancing caspase activation and modulating key apoptotic regulators, supporting its potential use in cancer treatment. However, further experimental validation is needed to confirm these interactions and their therapeutic implications.