Features of the complex of food additive hesperidin to hemoglobin.

The purpose of the current work was to examine the complexation of a mammalian protein, hemoglobin (Hb) with a food additive hesperidin at physiological conditions. Molecular modeling, fluorescence, and circular dichroism (CD) methods were exploited to analyze the binding domain, affinity, and the effects of hesperidin conjugation on Hb spatial structure. From molecular modeling, central cavity of Hb was assigned to retain high-affinity for hesperidin, this corroborates the steady state fluorescence and hydrophobic ANS probe results. The association of hesperidin with Hb emerges fluorescence quenching via static type, this phenomenon display that the ground state complex formation with an affinity of 10(4)M(-1), and hypsochromic effect transpires. Additionally, the alterations of synchronous fluorescence, CD, and three-dimensional fluorescence suggest that the polypeptide chain of Hb partially folding after conjugation with hesperidin. The above data suggest that Hb plays a significant role in the plasma distribution and transportation of hesperidin and related dietary flavonoids.