Characterization of the mangiferin-human serum albumin complex by spectroscopic and molecular modeling approaches.

The interactions between mangiferin and human serum albumin (HSA) were investigated by spectroscopy and molecular modeling. The results proved the formation of complex between mangiferin and HSA. Hydrophobic interaction dominated in the association reaction. Mangiferin statically quenched the fluorescence of HSA in a concentration dependent manner positively deviating from the linear Scatchard equation. The binding of mangiferin to HSA lead to changes in the conformation of HSA according to synchronous fluorescence spectra, FT-IR, UV-vis and CD data. The presence of amino acids and metal ion affected the binding constant of mangiferin-HSA complex. Computational mapping of the possible binding sites of mangiferin revealed the molecule to be bound in the large hydrophobic cavity of subdomain IIA.