Mangiferin binding to serum albumin is non-saturable and induces conformational changes at high concentrations

► The MGF-BSA complex exhibited positive cooperativity beyond 1:1 stoichiometry. ► The interaction of MGF with BSA is non-saturable at higher ligand concentration. ► The binding was accomplished by H-bonding, hydrophobic and electrostatic forces. ► The apparent binding constant for MGF-BSA was 0.38 mmol L−1. ► MGF binds electrostatically to BSA, different from a hydrophobic interaction to HSA.