Investigation of the binding interactions of Bisdemethoxycurcumin, Diacetylcurcumin and Diacetylbisdemethoxycurcumin with bovine α-lactalbumin by experimental and theoretical analysis

References

• Banji, D., Pinnapureddy, J., Banji, O. J. F., Saidulu, A., & Hayath, Md. (2011). Synergistic activity of curcumin with methotrexate in ameliorating Freund’s Complete Adjuvant induced arthritis with reduced hepatotoxicity in experimental animals. European Journal of Pharmacology, 668, 293–298.10.1016/j.ejphar.2011.06.006
   PubMed Web of Science ®Google Scholar
• Barbana, C., & Pérez, M. D. (2011). Interaction of α-lactalbumin with lipids and possible implications for its emulsifying properties – A review. International Dairy Journal, 21, 727–741.10.1016/j.idairyj.2011.04.009
   Web of Science ®Google Scholar
• Berliner, L. J., Ellis, P. D., & Murakami, K. (1983). Manganese(II) electron spin resonance and cadmium-113 nuclear magnetic resonance evidence for the nature of the calcium binding site in alpha-lactalbumins. Biochemistry, 22, 5061–5063.10.1021/bi00291a002
   PubMed Web of Science ®Google Scholar
• Browne, W. J., North, A. C. T., & Phillips, D. C. (1969). A possible three-dimensional structure of bovine α-lactalbumin based on that of hen’s egg-white lysozyme. Journal of Molecular Biology, 42, 65–86.10.1016/0022-2836(69)90487-2
   PubMed Web of Science ®Google Scholar
• Cawthern, K. M., Narayan, N., Chaudhuri, D., Permyakov, E. A., & Berliner, L. J. (1998). Interactions of a-lactalbumin with fatty acids and spin label analogs. The Journal of biological chemistry, 272, 30812–30816.
   Web of Science ®Google Scholar
• Chamani, J. (2010). Energetic domains analysis of bovine α-lactalbumin upon interaction with copper and dodecyl trimethylammonium bromide. Journal of Molecular Structure, 979, 227–234.10.1016/j.molstruc.2010.06.035
   Web of Science ®Google Scholar
• Chaudhuri, A., & Chattopadhyay, A. (2014). Lipid binding specificity of bovine α-lactalbumin: A multidimensional approach. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1838, 2078–2086.10.1016/j.bbamem.2014.04.027
   PubMed Web of Science ®Google Scholar
• Dewit, J. N. (1988). Nutritional and functional characteristics of whey proteins in food products. Journal of Dairy Science, 81, 597–608.
   Google Scholar
• Dzwolak, W. M., Shimizu, K. M., & Taniguchi, Y. (1999). Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine α-lactalbumin: The stabilizing role of the calcium ion. Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology, 1433, 45–55.10.1016/S0167-4838(99)00150-8
   PubMed Web of Science ®Google Scholar
• Farkas, V., Vass, E., Hanssen, I., Majer, Z., & Hollosi, M. (2005). Cyclic peptide models of the Ca2+ binding loop of α-lactalbumin. Bioorganic & Medicinal Chemistry, 13, 5310–5320.10.1016/j.bmc.2005.06.040
   PubMed Web of Science ®Google Scholar
• Gardikis, K., Hatziantoniou, S., Viras, K., & Demetzos, C. (2006). Effect of a bioactive curcumin derivative on DPPC membrane : A DSC and Raman spectroscopy study. Thermochimica Acta, 447, 1–4.10.1016/j.tca.2006.03.007
   Web of Science ®Google Scholar
• Gu, Q., & Kenny, J. E. (2009). Improvement of inner filter effect correction based on determination of effective geometric parameters using a conventional fluorimeter. Analytical Chemistry, 81, 420–426.10.1021/ac801676j
   PubMed Web of Science ®Google Scholar
• Guna Sekhar, P. M., & Prakash, V. (2008). Interaction of selected cosolvents with bovine α-lactalbumin. International Journal of Biological Macromolecules, 42, 348–355.10.1016/j.ijbiomac.2008.01.004
   PubMed Web of Science ®Google Scholar
• Hendrix, T., Griko, Y. V., & Privalov, P. L. (2000). A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin. Biophysical Chemistry, 84, 27–34.10.1016/S0301-4622(99)00140-4
   PubMed Web of Science ®Google Scholar
• Housaindokht, M. R., Chamani, J., & Moosavi-Movahedi, A. A. (2005). A differential scanning calorimetric study of the influence of copper and dodecyl trimethyl ammonium bromide on the stability of bovine α lactalbumin. International Journal of Biological Macromolecules, 36, 169–175.10.1016/j.ijbiomac.2005.05.005
   PubMed Web of Science ®Google Scholar
• Housaindokht, M. R., Chamani, J., Saboury, A. A., Moosavi-Movahedi, A. A., & Bahrololoom, M. (2001). Three binding sets analysis of α-lactalbumin by interaction of tetradecyl trimethyl ammonium bromide. Bulletin of the Korean Chemical Society, 22, 145–148.
   Web of Science ®Google Scholar
• Jayaprakasha, G. K., Jaganmohan Rao, L., & Sakariah, K. K. (2006). Antioxidant activities of curcumin, demethoxycurcumin and bisdemethoxycurcumin. Food Chemistry, 98, 720–724.10.1016/j.foodchem.2005.06.037
   Web of Science ®Google Scholar
• Jiao, Y., Wilkinson, J., Christine Pietsch, E., & Buss, J. L. (2006). Iron chelation in the biological activity of curcumin. Free Radical Biology & Medicine, 40, 1152–1160.10.1016/j.freeradbiomed.2005.11.003
   PubMed Web of Science ®Google Scholar
• Khorsand Ahmadi, A., Mahmoodian Moghadama, A., Mokaberia, P., Saberi, M., & Chamani, J. (2015). A comparison study of the interaction between β-lactoglobulin and retinol at two different conditions: Spectroscopic and molecular modeling approaches. Journal of Biomolecular Structure and Dynamics, 33, 1880–1898.10.1080/07391102.2014.977351
   PubMed Web of Science ®Google Scholar
• Lacowics, J. R. (1999). Principles of fluorescence spectroscopy. New York, NY: Kluwer Academic.
   Google Scholar
• Mohammadi, F., Bordbar, A. K., Divsalar, A., Mohammadi, K., & Saboury, A. A. (2009a). Analysis of binding interaction of curcumin and diacetylcurcumin with human and bovine serum albumin using fluorescence and circular dichroism spectroscopy. The Protein Journal, 28, 189–196.10.1007/s10930-009-9184-1
   PubMed Web of Science ®Google Scholar
• Mohammadi, F., Bordbar, A. K., Divsalar, A., Mohammadi, K., & Saboury, A. A. (2009b). Interaction of curcumin and diacetylcurcumin with the lipocalin member β-lactoglobulin. The Protein Journal, 28, 117–123.10.1007/s10930-009-9171-6
   PubMed Web of Science ®Google Scholar
• Mohammadi, F., Bordbar, A. K., Divsalar, A., Mohammadi, K., & Saboury, A. A. (2010). Circular dichroism and fluorescence spectroscopic study on the interaction of bisdemethoxycurcumin and diacetylbisdemethoxycurcumin with human serum albumin. Canadian Journal of Chemistry, 88, 155–163.10.1139/V09-169
   Web of Science ®Google Scholar
• Mohammadi, F., & Moeeni, M. (2015a). Analysis of binding interaction of genistein and kaempferol with bovine α-lactalbumin. Journal of Functional Foods, 12, 458–467.10.1016/j.jff.2014.12.012
   Web of Science ®Google Scholar
• Mohammadi, F., & Moeeni, M. (2015b). Study on the interactions of trans-resveratrol and curcumin with bovine α-lactalbumin by spectroscopic analysis and molecular docking. Materials Science and Engineering C, 50, 358–366.10.1016/j.msec.2015.02.007
   PubMed Web of Science ®Google Scholar
• Mohammadi, K., Thompson, K. H., Patrick, B. O., Storr, T., Martins, C., Polishchuk, E., … Orvig, C. (2005). Synthesis and characterization of dual function vanadyl, gallium and indium curcumin complexes for medicinal applications. Journal of Inorganic Biochemistry, 99, 2217–2225.10.1016/j.jinorgbio.2005.08.001
   PubMed Web of Science ®Google Scholar
• Noyelle, K., & Van Dael, H. (2002). Kinetics of conformational changes induced by the binding of various metal ions to bovine α-lactalbumin. Journal of Inorganic Biochemistry, 88, 69–76.10.1016/S0162-0134(01)00343-9
   PubMed Web of Science ®Google Scholar
• Payamkov, E. A., & Berliner, L. J. (2000). α-Lactalbumin: Structure and function. FEBS Letters, 473, 269–274.
   PubMed Web of Science ®Google Scholar
• Permyakov, E. A., & Berliner, L. J. (1994). Co2+ binding to α-lactalbumin. Journal of Protein Chemistry, 13, 277–281.10.1007/BF01901560
   PubMedGoogle Scholar
• Permyakov, E. A., Kalinichenko, L. P., Morozova, L. A., Yarmolenko, V. V., & Burstein, E. A. (1981). Calcium binding to α-lactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes. Biochemical and Biophysical Research Communications, 100, 191–197.10.1016/S0006-291X(81)80081-2
   PubMed Web of Science ®Google Scholar
• Permyakov, E. A., Morozova, L. A., & Burstein, E. A. (1985). Cation binding effects on the pH, thermal and urea denaturation transitions in alpha-lactalbumin. Biophysical Chemistry, 21, 21–31.
   PubMed Web of Science ®Google Scholar
• Rahnama, E., Mahmoodian-Moghaddamam, M., Khorsand-Ahmadia, S., Saberi, M., & Chamani, J. (2015). Binding site identification of metformin to human serum albumin and glycated human serum albumin by spectroscopic and molecular modeling techniques: A comparison study. Journal of Biomolecular Structure and Dynamics, 33, 513–533.10.1080/07391102.2014.893540
   PubMed Web of Science ®Google Scholar
• Rasmussen, B. W., & Bjerrum, M. J. (2003). Ca2+ and Na+ binding to high affinity sites of calcium-containing proteins measured by capillary electrophoresis. Journal of Inorganic Biochemistry, 95, 113–123.10.1016/S0162-0134(03)00093-X
   PubMed Web of Science ®Google Scholar
• Ravindran, J., Subbaraju, G. V., Ramani, M. V., Sung, B., & Aggarwal, B. B. (2010). Bisdemethylcurcumin and structurally related hispolon analogues of curcumin exhibit enhanced prooxidant, anti-proliferative and anti-inflammatory activities in vitro. Biochemical Pharmacology, 79, 1658–1666.10.1016/j.bcp.2010.01.033
   PubMed Web of Science ®Google Scholar
• Sattar, Z., Saberi, M., & Chamani, J. (2014). Determination of LMF binding site on a HSA-PPIX complex in the presence of human holo transferrin from the viewpoint of drug loading on proteins. PLoS One, 9, e84045.
   PubMed Web of Science ®Google Scholar
• Schaer, J. J., Miles, M., & Cox, J. X. (1985). Thermodynamics of the binding of calcium and strontium to bovine α-lactalbumin. FEBS Letters, 190, 77–80.10.1016/0014-5793(85)80431-2
   PubMed Web of Science ®Google Scholar
• Selvam, C., Chakrabortib, A. K., Jachak, S. M., & Thilagavathib, R. (2005). Design, synthesis, biological evaluation and molecular docking of curcumin analogues as antioxidant, cyclooxygenase inhibitory and anti-inflammatory agents. Bioorganic & Medicinal Chemistry Letters, 15, 1793–1797.10.1016/j.bmcl.2005.02.039
   PubMed Web of Science ®Google Scholar
• Stanciuc, N., & Papeanu, G. (2010). An overview of bovine α-lactalbumin structure and functionality. Food Technology, 34, 82–93.
   Google Scholar
• Takase, K., Niki, R., & Arima, S. (1978). Environment of Tryptophan Residues in α-Lactalbumin. The Journal of Biochemistry, 83, 371–378.
   PubMed Web of Science ®Google Scholar
• Vekshin, N. L. (1996). Separation of the tyrosine and tryptophan components of fluorescence using synchronous scanning method. Biofizika, 41, 1179–1179.
   Google Scholar
• Velusamy, V., & Palanipaan, L. (2011). Compositional analysis α-lactalbumin. American Journal of Biochemistry and Molecular Biology, 1, 106–120.
   Google Scholar
• Wang, Y. J., Pan, M. H., Cheng, A. L., Lin, L. I., Ho, Y. S., Hsieh, C. Y., & Lin, J. K. (1997). Stability of curcumin in buffer solutions and characterization of its degradation products. Journal of Pharmaceutical and Biomedical Analysis, 15, 1867–1876.10.1016/S0731-7085(96)02024-9
   PubMed Web of Science ®Google Scholar
• Ware, W. R. (1962). Oxygen quenching of fluorescence in solution: An experimental study of the diffusion process. The Journal of Physical Chemistry, 66, 455–458.10.1021/j100809a020
   Web of Science ®Google Scholar
• Warme, P. K., Momany, F. A., Rumball, S. V., Tuttle, R. W., & Scheraga, H. A. (1974). Computation of structures of homologous proteins. A-lactalbumin from lysozymet. Biochemistry, 13, 768–782.10.1021/bi00701a020
   PubMed Web of Science ®Google Scholar
• Xia, J., Mao, F., Yang, F., Zhao, Y., Zhang, C., & Yamamoto, K. (2011). Interaction of dietary polyphenols with bovine milk proteins: Molecular structure-affinity relationship and influencing bioactivity aspects. Molecular Nutrition & Food Research, 55, 1637–1645.10.1002/mnfr.v55.11
   PubMed Web of Science ®Google Scholar
• Yu, H., & Huang, Q. (2010). Enhanced in vitro anti-cancer activity of curcumin encapsulated in hydrophobically modified starch. Food Chemistry, 119, 669–674.10.1016/j.foodchem.2009.07.018
   Web of Science ®Google Scholar