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

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

Biophysics Division, Saha Institute of Nuclear Physics, Kolkata, India.
Department of Chemistry, Tougaloo College, Tougaloo, USA.
Department of Physics, Tougaloo College, Tougaloo, USA..
Saroj Mohan Institute of Technology, Hooghly, West Bengal, India;Department of Physics, Tougaloo College, Tougaloo, USA..

DOI: 10.4236/fns.2013.48A011                

Abstract

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 ? away from the closest heme group of chain α1, emphasizing the fact that the drug does not interfere with oxygen binding site of HbA.

Keywords

Natural Drug Carrier; Fluorescence; Circular Dichroism; Molecular Dynamics; Docking

Conflicts of Interest

The authors declare no conflicts of interest.

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