Lactoferrin is an iron-binding glycoprotein that supports innate immune defense, antimicrobial activity, and immune homeostasis
[1][2]. Mechanistically, lactoferrin links iron sequestration with host-cell signaling, and studies describe effects on antigen-presenting cells, cytokine balance, and LPS-responsive inflammatory pathways
[2][3][4]. In epithelial and macrophage inflammatory models, lactoferrin attenuates LPS-stimulated inflammatory responses and barrier impairment through NF-κB, MAPK, and Nrf2 pathway modulation
[3][4]. In cancer models, bovine or recombinant human lactoferrin induces cell-cycle arrest, disrupts cytoskeletal organization, inhibits mTOR signaling, or promotes apoptosis in selected breast cancer cells
[5][6]. Compared with related lactoferrin-derived peptides, intact lactoferrin provides the broader iron-binding and immune-modulatory scaffold, whereas lactoferricin and lactoferrampin are N-terminal antimicrobial peptides with antibacterial, antiviral, antifungal, and anti-inflammatory activities
[7][8]. For experimental applications, lactoferrin-derived peptide chimeras show stronger membrane-perturbing antimicrobial activity than individual peptides, making them useful tools for structure-activity and membrane-interaction studies
[8].