Abstract
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.