Abstract
This study investigates the comprehensive characterization of the interaction between β-lactoglobulin (β-LG) and Silibinin using various spectroscopic techniques. Fluorescence quenching experiments at different temperatures (298, 303, 308, and 313 K) revealed substantive interactions between β-LG and Silibinin, as indicated by a reduction in fluorescence intensity and a red shift in emission maxima. Further analysis, including Stern-Volmer quenching constants (KSV), bimolecular quenching rate constants (kq), and thermodynamic parameters demonstrated static quenching mechanism and strong binding affinities (Ka range: 0.138–1.483 × 105 M−1) between BLG-Silibinin complex. Thermodynamic study suggested positive enthalpy and entropy changes (ΔHo=43.31 kcal mol−1; ΔSo=164.33 cal mol−1 K−1), suggesting a spontaneous reaction with negative ΔGo values (-5.66 to -7.30 kcal mol−1). Forster resonance energy transfer (FRET) measurements confirmed optimal distances (r and Ro) for FRET occurrence, endorsing the static quenching mechanism. Molecular docking supported these findings, showcasing a 1:1 stoichiometric binding ratio for β-LG: Silibinin. The β-LG and Silibinin complex is primarily stabilized by hydrogen bonds and hydrophobic interactions. Molecular dynamics simulations over 200 ns highlighted stability in the β-LG-Silibinin complex, indicated by RMSD convergence, consistent RMSF values, and compactness illustrated by Rg. Conformational changes in β-LG upon Silibinin binding were further confirmed through UV-Vis absorption spectroscopy, FTIR, far-UV CD, synchronous fluorescence, and 3D fluorescence analyses. Functionally, the antioxidant capacity of β-LG increased after complexation with silibinin as quantified by DPPH assay. These results collectively depict the intricate network of interactions between Silibinin and β-LG, shedding light on the molecular details of their binding and offering insights into potential functional implications in biological contexts.
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