Interactions between β-Lactoglobulin and 3,3'-Diindolylmethane in Model System.

Area of Science:

• Biochemistry
• Materials Science
• Pharmacology

Background:

• 3,3 -diindolylmethane (DIM) exhibits broad-spectrum anticancer activities.
• Limited stability and bioavailability hinder the therapeutic application of DIM.
• Whey proteins, like β-lactoglobulin (β-LG), are potential candidates for developing drug delivery systems.

Purpose of the Study:

• To investigate the interaction between DIM and β-LG.
• To explore the potential of β-LG as a carrier for DIM.
• To characterize the formation and properties of DIM-β-LG nanocomplexes.

Main Methods:

• UV-Vis absorption spectroscopy to detect complex formation.
• Fluorescence spectroscopy to determine binding constants.
• Circular dichroism and FT-IR spectroscopy to analyze structural changes.
• Molecular docking simulations to elucidate interaction mechanisms.

Main Results:

• DIM binding increased β-LG particle size and zeta potential, indicating complex formation.
• Spectroscopic data confirmed the formation of a DIM-β-LG complex with a binding constant of 6.7 × 10^5 M⁻¹.
• Structural analysis revealed alterations in β-LG secondary structure (decreased helix/turn, increased β-sheet/unordered) upon DIM interaction.
• Hydrophobic interactions and hydrogen bonds were identified as key forces in forming DIM-β-LG nanocomplexes.

Conclusions:

• β-LG effectively binds to DIM, forming stable nanocomplexes.
• The structural changes in β-LG upon binding suggest a protective effect on DIM.
• β-LG shows significant potential as a protein-based vehicle for DIM protection and delivery, enhancing its therapeutic applicability.