Study of the interaction between DNP and DIDS with human hemoglobin as binary and ternary systems: spectroscopic and molecular modeling investigation

References

• Anbazhagan, V., & Renganathan, R. (2008). Study on the binding of 2,3-diazabicyclo[2.2.2]oct-2-ene with bovine serum albumin by fluorescence spectroscopy. Journal of Luminescence, 128, 1454–1458.
   Web of Science ®Google Scholar
• Bao, X. Y., Zhu, Z. W., Li, N. Q., & Chen, J. G. (2001). Electrochemical studies of rutin interacting with hemoglobin and determination of hemoglobin. Talanta, 54, 591–596.
   PubMed Web of Science ®Google Scholar
• Bi, S. Y., Song, D. Q., Tian, Y., Zhou, X., Liu, Z., & Zhang, H. (2005). Molecular spectroscopic study on the interaction of tetracyclines with serum albumins. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 61, 629–636.
   PubMed Web of Science ®Google Scholar
• Boys, B. L., & Konermann, L. (2007). Folding and assembly of hemoglobin monitored by electrospray mass spectrometry using an on-line dialysis system. Journal of the American Society for Mass Spectrometry, 18, 8–16.
   PubMed Web of Science ®Google Scholar
• Chen, G. Z., Huang, X. Z., Xu, J. G., Zheng, Z., & Wang, Z. B. (1990). The method of fluorescence analysis (2nd ed.). Beijing: Science Press.
   Google Scholar
• Chen, Q., Lalezari, I., Nagel, R. L., & Hirsch, R. E. (2005). Liganded hemoglobin structural perturbations by the allosteric effector L35. Biophysical Journal, 88, 2057–2067.
   PubMed Web of Science ®Google Scholar
• Chen, L., & Tianqing, L. (2008). Interaction behaviors between chitosan and hemoglobin. International Journal of Biological Macromolecules, 42, 441–446.
   PubMed Web of Science ®Google Scholar
• Chi, Z., Liu, R., Yang, B., & Zhang, H. (2010). Toxic interaction mechanism between oxytetracycline and bovine hemoglobin. Journal of Hazardous Materials, 180, 741–747.
   PubMed Web of Science ®Google Scholar
• Cui, F. L., Fan, J. J., Li, J. P., & Hu, Z. D. (2004). Interactions between 1-benzoyl-4-p-chlorophenyl thiosemicarbazide and serum albumin: Investigation by fluorescence spectroscopy. Bioorganic & Medicinal Chemistry, 12, 151–157.
   PubMed Web of Science ®Google Scholar
• Cui, F., Zhang, Q., Yao, X., Luo, H., Yang, Y., Qin, L., … Lu, Y. (2008). The investigation of the interaction between 5-Iodouracil and human serum albumin by spectroscopic and modeling methods and determination of protein by synchronous fluorescence technique. Biochemistry & Physiology, 90, 126–134.
   Web of Science ®Google Scholar
• Ding, F., Liu, W., Zhang, X., & Zhang, L. (2010). Fluorescence and circular dichroism studies of conjugates between metsulfuron-methyl and human serum albumin. Colloids and Surfaces B: Biointerfaces, 76, 441–448.
   PubMed Web of Science ®Google Scholar
• Divya, O., & Mishra, A. K. (2008). Understanding the concept of concentration-dependent red-shift in synchronous fluorescence spectra: Prediction of and optimization of Δλ for synchronous fluorescence scan. Analytica Chimica Acta, 630, 47–56.
   PubMed Web of Science ®Google Scholar
• Donskova, E. N., Stasovskaya, V. V., & Repko, L. I. (1975). Application of pulse conductometry to the determination of the particle size distributions of metal powders. Powder Metallurgy, 14, 863–865.
   Google Scholar
• Hals, G. D., & Palade, P. T. (1990). Different sites control voltage dependence and conductance of sarcoball anion channel. Biophysical Journal, 57, 1037–1047.
   PubMed Web of Science ®Google Scholar
• He, X. M., & Carter, D. C. (1992). Atomic structure and chemistry of human serum albumin. Nature, 358, 209–223.
   PubMed Web of Science ®Google Scholar
• Jang, J., Liu, H., Chen, W., & Zou, G. (2009). Binding of mitomycin C to blood proteins: A spectroscopic analysis and molecular docking. Journal of Molecular Structure, 928, 72–77.
   Web of Science ®Google Scholar
• Kabiri, M., Amiri-Tehranizadeh, Z., Baratian, A., Saberi, M. R., & Chamani, J. (2012). Use of spectroscopic, zeta potential and molecular dynamic techniques to study the interaction between human holo-transferrin and two antagonist drugs: Comparison of binary and ternary systems. Molecules, 17, 3114–3147.
   PubMed Web of Science ®Google Scholar
• Kawasaki, T., & Kasai, M. (1989). Disulfonicstilbene derivatives open the Ca2+ release channel of sarcoplasmic reticulum. Journal of Biochemistry, 106, 401–405.
   PubMed Web of Science ®Google Scholar
• Kerec, M., Bogataj, M., Mugerle, B., Gaperlin, A., & Mrhar, A. (2002). Mucoadhesion on pig vesical mucosa: Influence of polycarbophil/calcium interactions. International Journal of Pharmaceutics, 241, 135–143.
   PubMed Web of Science ®Google Scholar
• Laib, S., & Seeger, S. (2004). FRET studies of the interaction of dimeric cyanine dyes with DNA. Journal of Fluorescence, 14, 187–191.
   PubMed Web of Science ®Google Scholar
• Lakowicz, J. R. (1999). Principles of fluorescence spectroscopy. New York: Kluwer Academic / Plenum Press. p. 37.
   Google Scholar
• Lakowicz, J. R. (2006). Principles of fluorescence spectroscopy. New York: Springer Science, Business Media. pp. 52, 277 and 530.
   Google Scholar
• Lei, C., Wollenberger, U., Bistolas, N., Guiseppi-Elie, A., & Scheller, F. W. (2002). Electron transfer of hemoglobin at electrodes modified with colloidal clay nanoparticles. Analytical and Bioanalytical Chemistry, 372, 235–239.
   PubMed Web of Science ®Google Scholar
• Lu, J. Q., Jin, F., Sun, T. Q., & Zhou, X. W. (2007). Multi-spectroscopic study on interaction of bovine serum albumin with lomefloxacin–copper(II) complex. International Journal of Biological Macromolecules, 40, 299–304.
   PubMed Web of Science ®Google Scholar
• Maciazel-Jurczyk, M., Sulkowsla, A., Bojko, B., Rownicka, J., & Sulkowski, W. (2009). Interaction of phenylbutazone and colchicine in binding to serum albumin in rheumatoid therapy, 1H NMR study. Journal of Molecular Structure, 74, 1–9.
   Google Scholar
• Mandal, P., Bardhan, M., & Ganguly, T. (2010). A detailed spectroscopic study on the interaction of Rhodamine 6G with human hemoglobin. Journal of Photochemistry and Photobiology B: Biology, 99, 78–86.
   PubMed Web of Science ®Google Scholar
• Mark, A., Hink-Nina, V., Borst, V. J. W., Hoek, A. v., & Visser, A. J. W. G. (2003). Practical use of corrected fluorescence excitation and emission spectra of fluorescent proteins in Förster Resonance Energy Transfer (FRET) studies. Journal of Fluorescence, 13, 185–188.
   Web of Science ®Google Scholar
• Mohammed-Sultan, N. A., Rao, R. N., Nadimpalli, S. K., & Swamy, M. J. (2006). Tryptophan environment, secondary structure and thermal unfolding of the galactose-specific seed lectin from Dolichos lablab: fluorescence and circular dichroism spectroscopic studies. Biochimica et Biophysica Acta, Proteins and Proteomics, 1760, 1001–1008.
   Web of Science ®Google Scholar
• Moreno, F., & González-Jiménez. (1999). Binding of the Promen fluorescent probe to human serum albumin. Chemico-Biological Interactions, 121, 237–252.
   PubMed Web of Science ®Google Scholar
• Pan, X., Liu, J., Zhang, D., Chen, X., Song, W., & Wu, F. (2010). Binding of dicamba to soluble and bound extracellular polymeric substances (EPS) from aerobic activated sludge: A fluorescence quenching study. Journal of Colloid and Interface Science, 345, 442–447.
   PubMed Web of Science ®Google Scholar
• Peterlin, P. (2010). Frequency-dependent electrodeformation of giant phospholipid vesicles in AC electric field. Journal of Biological Physics, 36, 339–354.
   PubMed Web of Science ®Google Scholar
• Pinho Melo, E. P., Aires-Barros, M. R., Costa, S. M., & Cabral, J. M. (1997). Thermal unfolding of proteins at high pH range studied by UV absorbance. Journal of Biochemical and Biophysical Methods, 34, 45–59.
   PubMedGoogle Scholar
• Ravasi, D., Masserini, M., Vecchio, G., Li, Y. T., & Li, S. Ch. (2002). Study of interaction of GM2 activator protein with GM2 using circular dichroism and fluorescence spectroscopy. Neurochemical Research, 27, 785–792.
   PubMed Web of Science ®Google Scholar
• Sarzehi, S., & Chamani, J. (2010). Investigation on the interaction between tamoxifen and human holo-transferrin: Determination of the binding mechanism by fluorescence quenching, resonance light scattering and circular dichroism methods. International Journal of Biological Macromolecules, 47, 558–569.
   PubMed Web of Science ®Google Scholar
• Shcharbin, D., Janicka, M., Wasiak, M., Palecz, B., Przybyszewska, M., Zaborski, M., & Bryszewska, M. (2007). Serum albumins have five sites for binding of cationic dendrimers. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1774, 946–951.
   PubMed Web of Science ®Google Scholar
• Shen, X. C., Liou, X. Y., Ye, L. P., Liang, H., & Wang, Z. Y. (2007). Spectroscopic studies on the interaction between human hemoglobin and CdS quantum dots. Journal of Colloid and Interface Science, 311, 400–406.
   PubMed Web of Science ®Google Scholar
• Silva, D., Cortez, C. M., & Cunha-Bastos, J. (2004). Methyl parathion interaction with human and bovine serum albumin. Toxicology Letters, 147, 53–61.
   PubMed Web of Science ®Google Scholar
• Sklar, L. A., Hudson, B. S., & Simoni, R. D. (1977). Conjugated polyene fatty acids as fluorescent probes: Binding to bovine serum albumin. Biochemistry, 16, 5100–5108.
   PubMed Web of Science ®Google Scholar
• Swati, D. e., & Agnishwar, G. (2006). A fluorimetric and circular dichroism study of hemoglobin – Effect of pH and anionic amphiphiles. Journal of Colloid and Interface Science, 296, 324–331.
   PubMed Web of Science ®Google Scholar
• Tang, Y. J., Chen, Y., Chen, Z., Xie, T. T., & Li, Y. Q. (2008). Adsorption of a protein–porphyrin complex at a liquid–liquid interface studied by total internal reflection synchronous fluorescence spectroscopy. Analytica Chimica Acta, 614, 71–76.
   PubMed Web of Science ®Google Scholar
• Tang, J., Luan, F., & Chen, X. (2006). Binding analysis of glycyrrhetinic acid to human serum albumin: Fluorescence spectroscopy, FTIR, and molecular modeling. Journal of Bioorganic & Medicinal Chemistry, 14, 3210–3217.
   PubMed Web of Science ®Google Scholar
• Wang, L., Liu, R., Chi, Z., Yang, B., Zhang, P., & Wang, M. (2010). Spectroscopic investigation on the toxic interactions of Ni2+ with bovine hemoglobin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 76, 155–160.
   PubMed Web of Science ®Google Scholar
• Wang, Z. J., Ren, L. X., Zhao, Y. Q., Li, G. T., Duan, L., Liang, A. H., & Yang, B. S. (2008). Investigation on the binding of TNS to centrin, an EF-hand protein. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 70, 892–897.
   PubMed Web of Science ®Google Scholar
• Wang, Y. Q., Tang, B. P., Zhang, H. M., Zhou, Q. H., & Zhang, G. C. (2009). Studies on the interaction between imidacloprid and human serum albumin: Spectroscopic approach. Journal of Photochemistry and Photobiology B: Biology, 94, 183–190.
   PubMed Web of Science ®Google Scholar
• Wang, Y. Q., Zhang, H. M., Zhang, G. C., Liu, S. X., Zhou, Q. H., Fei, Z. H., & Liu, Z. T. (2007). Studies of the interaction between paraquat and bovine hemoglobin. International Journal of Biological Macromolecules, 41, 243–250.
   PubMed Web of Science ®Google Scholar
• Wang, Y. Q., Zhang, H. M., & Zhou, Q. H. (2009). Studies on the interaction of caffeine with bovine hemoglobin. European Journal of Medicinal Chemistry, 44, 2100–2105.
   PubMed Web of Science ®Google Scholar
• Wang, Y. Q., Zhang, H. M., Zhou, Q. H., & Xu, H. L. (2008). A study of the binding of colloidal Fe3O4 with bovine hemoglobin using optical spectroscopy. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 237, 139–147.
   Google Scholar
• Wu, T., Wu, Q., Guan, S., Su, H., & Cai, Z. (2007). Binding of the environmental pollutant naphthol to bovine serum albumin. Biomacromolecules, 8, 1899–1906.
   PubMed Web of Science ®Google Scholar
• Xiao, J., Shi, J., Cao, H., Wu, S., Ren, F., & Xu, M. (2007). Analysis of binding interaction between puerarin and bovine serum albumin by multi-spectroscopic method. Journal of Pharmaceutical and Biomedical Analysis, 45, 609–615.
   PubMed Web of Science ®Google Scholar
• Yuan, J. L., Liu, H., Kang, X., Lv, Z., & Zou, G. L. (2008). Characteristics of the isomeric flavonoids apigenin and genistein binding to hemoglobin by spectroscopic methods. Journal of Molecular Structure, 891, 333–339.
   Web of Science ®Google Scholar
• Zhang, H., Hassanali, A. A., Shin, Y. K., Knight, C., & Singer, S. J. (2011). The water–amorphous silica interface: Analysis of the Stern layer and surface conduction. The Journal of Chemical Physics, 134, 024705–24712.
   PubMed Web of Science ®Google Scholar
• Zhang, D., Pan, X., Mostofa, K. M. G., Chen, X., Mu, G., Wu, F., … Fu, Q. (2010). Complexation between Hg(II) and biofilm extracellular polymeric substances: An application of fluorescence spectroscopy. Journal of Hazardous Materials, 175, 359–365.
   PubMed Web of Science ®Google Scholar
• Zhang, G., Que, Q., Pan, J., & Guo, J. (2008). Study of the interaction between icariin and human serum albumin by fluorescence spectroscopy. Journal of Molecular Structure, 881, 132–138.
   Web of Science ®Google Scholar
• Zhang, H. N., Wang, Y. Q., & Zhou, Q. H. (2009). Molecular interaction between phosphomolybdate acid and bovine hemoglobin. Journal of Molecular Structure, 921, 156–162.
   Web of Science ®Google Scholar
• Zhou, Q. H., Wang, Y. Q., Zhang, H. M., Zhang, G. C., Fei, Z. H., & Liu, Z. T. (2007). Studies of the interaction between paraquat and bovine hemoglobin. Journal of Instrumental Analysis, 41, 243–250.
   Google Scholar
• Zhou, J., Wu, X., Gu, X., Zhou, L., Song, K., & Wei, S. (2009). Spectroscopic studies on the interaction of hypocrellin A and hemoglobin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 72, 151–155.
   PubMed Web of Science ®Google Scholar