Research ArticleOpen AccessGoogle Scholar indexed
Biophysical Characterization of Genistein in Its Natural Carrier Human Hemoglobin Using Spectroscopic and Computational Approaches
Biophysics Division, Saha Institute of Nuclear Physics, Kolkata, India
Saroj Mohan Institute of Technology, Hooghly, West Bengal, India;Department of Physics, Tougaloo College, Tougaloo, USA.
Department of Chemistry, Tougaloo College, Tougaloo, USA
Biophysics Division, Saha Institute of Nuclear Physics, Kolkata, India
Department of Chemistry, Tougaloo College, Tougaloo, USA
Department of Chemistry, Tougaloo College, Tougaloo, USA
Department of Chemistry, Tougaloo College, Tougaloo, USA
Department of Chemistry, Tougaloo College, Tougaloo, USA
Department of Physics, Tougaloo College, Tougaloo, USA.
Biophysics Division, Saha Institute of Nuclear Physics, Kolkata, India
Biophysics Division, Saha Institute of Nuclear Physics, Kolkata, India
- 1 Biophysics Division, Saha Institute of Nuclear Physics, Kolkata, India
- 2 Saroj Mohan Institute of Technology, Hooghly, West Bengal, India;Department of Physics, Tougaloo College, Tougaloo, USA.
- 3 Department of Chemistry, Tougaloo College, Tougaloo, USA
- 4 Biophysics Division, Saha Institute of Nuclear Physics, Kolkata, India
- 5 Department of Chemistry, Tougaloo College, Tougaloo, USA
- 6 Department of Chemistry, Tougaloo College, Tougaloo, USA
- 7 Department of Chemistry, Tougaloo College, Tougaloo, USA
- 8 Department of Chemistry, Tougaloo College, Tougaloo, USA
- 9 Department of Physics, Tougaloo College, Tougaloo, USA.
- 10 Biophysics Division, Saha Institute of Nuclear Physics, Kolkata, India
- 11 Biophysics Division, Saha Institute of Nuclear Physics, Kolkata, India
Food and Nutrition Sciences·Volume 04 (2013)·Pages 83–92·Published 26 July 2013·DOI10.4236/fns.2013.48A011
Copy link · social · email
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) × 10 4 M - 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 α 1, emphasizing the fact that the drug does not interfere with oxygen binding site of HbA.
KeywordsNatural Drug CarrierFluorescenceCircular DichroismMolecular DynamicsDocking
- St. Rusznyák and A. Szent-Gyorgyi, “Vitamin P: Flavonols as Vitamins,” Nature, Vol. 138, No. 3479, 1936, p. 27.
- S. Chaudhuri, A. Banerjee, K. Basu, B. Sengupta and P. K. Sengupta, “Interaction of Flavonoids with Red Blood Cell Membrane Lipids and Proteins: Antioxidant and Antihemolytic Effects,” International Journal of Biological Macromolecule, Vol. 41, No. 1, 2007, pp. 42-48. doi:10.1016/j.ijbiomac.2006.12.003
- B. Sengupta, T. Uematsu, P. Jacobsson and J. Swenson, “Exploring the Antioxidant Property of Bioflavonoid Quercetin in Preventing DNA Glycation: A Calorimetric and Spectroscopic Study,” Biochemical and Biophysical Research Communications, Vol. 339, No. 1, 2006, pp. 355361. doi:10.1016/j.bbrc.2005.11.019
- B. Sengupta and J. Swenson, “Properties of Normal and Glycated Human Hemoglobin in Presence and Absence of Antioxidant,” Biochemical and Biophysical Research Communications, Vol. 334, No. 3, 2005, pp. 954-959. doi:10.1016/j.bbrc.2005.06.181
- S. Chakraborty, S. Chaudhuri, B. Pahari, J. Taylor, P. K. Sengupta and B. Sengupta, “A Critical Study on the Interactions of Hesperitin with Human Hemoglobin: Fluorescence Spectroscopic and Molecular Modeling Approach,” Journal of Luminescence, Vol. 132, No. 6, 2012, pp. 15221528. doi:10.1016/j.jlumin.2012.01.021
- G. Rusak, H. O. Gutzeit and J. L. Müller, “Structurally Related Flavonoids with Antioxidative Properties Differentially Affect Cell Cycle Progression and Apoptosis of Human Acuteleukemia Cells,” Nutrition Research, Vol. 25, No. 2, 2005, pp. 143-155. doi:10.1016/j.nutres.2004.12.003
- A. Constantinou, K. Kiguchi and E. Huberman, “Induction of Differentiation and DNA Strand Breakage in Human HL-60 and K-562 Leukemia Cells by Genistein,” Cancer Research, Vol. 50, No. 9, 1990, pp. 2618-2624.
- D. A. Frank and A. C. Sartorelli, “Alterations in Tyrosine Phosphorylation during the Granulocytic Maturation of HL-60 Leukemia Cells,” Cancer Research, Vol. 48, No. 1, 1988, pp. 52-58.
- T. Akiyama, J. Ishida, S. Nakagawa, H. Ogawara, S.-I. Watanabe, N. Itoh, M. Shibuya and Y. Fukami, “Genistein, a Specific Inhibitor of Tyrosine-Specific Protein Kinases,” Journal of Biological Chemistry, Vol. 262, No. 12. 1987, pp. 5592-5595.
- K. Kiguchi, A. I. Constantinou and E. Huberman, “Genistein-Induced Cell Differentiation and Protein-Linked DNA Strand Breakage in Human Melanoma Cells,” Cancer Communications, Vol. 2, No. 8, 1990, pp. 271-277.
- A. Bolli, M. Marino, G. Rimbach, G. Fanali, M. Fasano and P. Ascenzi, “Flavonoid Binding to Human Serum Albumin,” Biochemical and Biophysical Research Communications, Vol. 398, No. 3, 2010, pp. 444-449. doi:10.1016/j.bbrc.2010.06.096