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Biophysical Characterization of Genistein in Its Natural Carrier Human Hemoglobin Using Spectroscopic and Computational Approaches

Author(s): Biswapathik Pahari | Sandipan Chakraborty | Bidisha Sengupta | Sudip Chaudhuri | William Martin | Jasmine Taylor | Jordan Henley | Donald Davis | Pradip K. Biswas | Amit K. Sharma | Pradeep K. Sengupta

Journal: Food and Nutrition Sciences
ISSN 2157-944X

Volume: 04;
Issue: 08;
Start page: 83;
Date: 2013;
Original page

Keywords: Natural Drug Carrier | Fluorescence | Circular Dichroism | Molecular Dynamics | Docking

Steady state and time resolved fluorescence spectroscopy, combined with molecular dynamics simulation, have been used to explore the interactions of a therapeutically important bioflavonoid, genistein, with normal human hemoglobin (HbA). Binding constants estimated from the fluorescence studies were K = (3.5 ± 0.32) ×104M-1 for genistein. Specific interactions with HbA were confirmed from flavonoid-induced fluorescence quenching of the tryptophan in the protein HbA. The mechanism of this quenching involves both static and dynamic components as indicated by: (a) increase in the values of Stern-Volmer quenching constants with temperatures, (b) / is slightly > 1 (where   and  are the unquenched and quenched tryptophan fluorescence lifetimes (averaged) respectively). Molecular docking and dynamic simulations reveal that genistein binds between the subunits of HbA, ~18 &Aring away from the closest heme group of chain α1, emphasizing the fact that the drug does not interfere with oxygen binding site of HbA.
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