Lactoferrin–beta-glucan supramolecular complex (LF-BG complex)

The Lactoferrin–beta-glucan supramolecular complex is a functional assembly formed through non-covalent interactions, such as electrostatic and hydrophobic forces, between the iron-binding glycoprotein lactoferrin and the immunomodulatory polysaccharide beta-glucan (Wang et al., 2022, Food Hydrocolloids). This complex is not a single biological target but rather a therapeutic delivery system or nutraceutical agent designed to enhance the stability and bioactivity of its individual components (Zhang et al., 2021, Journal of Agricultural and Food Chemistry). Beta-glucan acts as a protective carrier, shielding lactoferrin from gastric degradation and facilitating its delivery to the intestinal mucosa (Legrand, 2016, The Journal of Pediatrics). Once in the body, the complex interacts with various receptors, including Dectin-1 (the primary receptor for beta-glucan) and lactoferrin receptors like Intelectin-1 or LRP1, to modulate the immune system (Goodridge et al., 2009, Immunological Reviews). These interactions promote the activation of macrophages, neutrophils, and natural killer cells, leading to enhanced antimicrobial and anti-inflammatory effects (Kruzel et al., 2017, Frontiers in Immunology). Due to its synergistic properties, the complex is investigated for its potential in managing infections, chronic inflammation, and as a supportive therapy in oncology.

Other names

Lactoferrin-beta-glucan complexLF-BG supramolecular assemblyLactoferrin-beta-glucan nanoparticlesLactoferrin-beta-glucan conjugate

The complex functions as a bioactive delivery vehicle that protects lactoferrin from proteolysis while providing synergistic immunomodulation through the dual activation of Dectin-1 (by beta-glucan) and lactoferrin receptors such as Intelectin-1, enhancing cytokine production and innate immune cell activity.