β-Lactoglobulin complexation with phlorizin enhances intestinal accessibility and MUC2 secretion, reducing antigenicity.

Phlorizin (PZ), a naturally occurring flavonoid glycoside, holds promise as an antioxidant and antidiabetic agent. However, its clinical utility is severely hampered by poor aqueous solubility (<0.1 mg/mL) and suboptimal bioavailability. Addressing this, researchers are exploring protein carriers like β-lactoglobulin (β-LG), a whey protein known for its ability to transport hydrophobic nutrients and its immunomodulatory properties. This study investigates β-LG complexation as a strategy to overcome PZ's delivery limitations and enhance its therapeutic potential, particularly concerning intestinal health.

This study systematically characterized the PZ-β-LG complex by integrating computational simulations, spectroscopic validation, and in vitro functional assays. Molecular dynamics simulations elucidated the binding mechanism. Spectroscopic methods, including UV-Visible absorption and intrinsic fluorescence, validated the binding. Gastrointestinal stability was assessed using simulated digestion coupled with Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS) peptidomics. Cellular assessments utilized LS174T intestinal epithelium cells to evaluate PZ-associated cytotoxicity and the complex's synergistic effects on mucin-2 (MUC2) expression and secretion.