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The association of silybin with β-cyclodextrin and its influence on silybin’s binding with bovine serum albumin are reported. The stoichiometry, binding constant, and the structure of silybin–β-cyclodextrin inclusion complex are reported. The titrations of silybin with bovine serum albumin in the absence and presence of βcyclodextrin are carried out and the differences in binding strengths are discussed. Molecular modeling is used to optimize the sites and mode of binding of silybin with bovine serum albumin. Förster resonance energy transfer is calculated and the proximity of interacting molecules is reported in the presence and absence of βcyclodextrin.

Capping of Silybin with β-Cyclodextrin Influences its Binding with Bovine Serum Albumin: A Study by Fluorescence Spectroscopy and Molecular Modeling