Studying the interaction between three synthesized heterocyclic sulfonamide compounds with hemoglobin by spectroscopy and molecular modeling techniques

References

• Abbate, F., Casini, A., Owa, T., Scozzafava, A., & Supuran, C. T. (2004). Carbonic anhydrase inhibitors: E7070, a sulfonamide anticancer agent, potently inhibits cytosolic isozymes I and II, and transmembrane, tumor-associated isozyme IX. Bioorganic & Medicinal Chemistry Letters, 14, 217–223.10.1016/j.bmcl.2003.09.062
   PubMed Web of Science ®Google Scholar
• Abdollahpour, N., Asoodeh, A., Saberi, M. R., & Chamani, J. (2011). Separate and simultaneous binding effects of aspirin and amlodipine to human serum albumin based on fluorescence spectroscopic and molecular modeling characterizations: A mechanistic insight for determining usage drugs doses. Journal of Luminescence, 131, 1885–1899.10.1016/j.jlumin.2011.04.043
   Web of Science ®Google Scholar
• Ahmed, E. M., Taha, N. M., Abd El-Gawad, S. M., & Nady, N. M. S. (2011). Novel thiourea, quinazoline, thiazolidine, thieno[2,3-d]-pyrimidine, 4-thiazolidinone, pyrrole, pyrrolo[2,3-d]pyrimidine derivatives containing sulfamoyl moiety. Der Chemica Sinica, 2, 197–210.
   Google Scholar
• Alsughayer, A., Elassar, A.-Z. A., Mustafa, S., & Al Sagheer, F. (2011). Synthesis, structure analysis and antibacterial activity of new potent sulfonamide derivatives. Journal of Biomaterials and Nanobiotechnology, 2, 143.10.4236/jbnb.2011.22018
   Google Scholar
• Azimi, O., Emami, Z., Salari, H., & Chamani, J. (2011). Probing the interaction of human serum albumin with norfloxacin in the presence of high-frequency electromagnetic fields: Fluorescence spectroscopy and circular dichroism investigations. Molecules, 16, 9792–9818. doi:10.3390/molecules16129792
   PubMed Web of Science ®Google Scholar
• Barbero, N., Napione, L., Quagliotto, P., Pavan, S., Barolo, C., Barni, E., … Viscardi, G. (2009). Fluorescence anisotropy analysis of protein–antibody interaction. Dyes and Pigments, 83, 225–229.10.1016/j.dyepig.2009.04.011
   Web of Science ®Google Scholar
• Bensikaddour, H., Snoussi, K., Lins, L., Van Bambeke, F., Tulkens, P. M., Brasseur, R., … Mingeot-Leclercq, M.-P. (2008). Interactions of ciprofloxacin with DPPC and DPPG: Fluorescence anisotropy, ATR-FTIR and 31 P NMR spectroscopies and conformational analysis. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1778, 2535–2543.10.1016/j.bbamem.2008.08.015
   PubMed Web of Science ®Google Scholar
• Bloemendal, M., Toumadje, A., & Johnson, W. C. (1999). Bovine lens crystallins do contain helical structure: A circular dichroism study. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, 1432, 234–238.10.1016/S0167-4838(99)00107-7
   PubMed Web of Science ®Google Scholar
• Canet, D., Doering, K., Dobson, C. M., & Dupont, Y. (2001). High-sensitivity fluorescence anisotropy detection of protein-folding events: Application to α-lactalbumin. Biophysical Journal, 80, 1996–2003.10.1016/S0006-3495(01)76169-3
   PubMed Web of Science ®Google Scholar
• Chamani, J., Tafrishi, N., & Momen-Heravi, M. (2010). Characterization of the interaction between human lactoferrin and lomefloxacin at physiological condition: Multi-spectroscopic and modeling description. Journal of Luminescence, 130, 1160–1168.10.1016/j.jlumin.2010.02.014
   Web of Science ®Google Scholar
• Chaudhuri, S., Pahari, B., Sengupta, B., & Sengupta, P. K. (2010). Binding of the bioflavonoid robinetin with model membranes and hemoglobin: Inhibition of lipid peroxidation and protein glycosylation. Journal of Photochemistry and Photobiology B: Biology, 98, 12–19. doi:10.1016/j.jphotobiol.2009.10.002
   PubMed Web of Science ®Google Scholar
• Cheema, M. A., Taboada, P., Barbosa, S., Juárez, J., Gutiérrez-Pichel, M., Siddiq, M., & Mosquera, V. (2009). Human serum albumin unfolding pathway upon drug binding: A thermodynamic and spectroscopic description. The Journal of Chemical Thermodynamics, 41, 439–447.10.1016/j.jct.2008.11.011
   Web of Science ®Google Scholar
• Cui, F. L., Fan, 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, 151–157.10.1016/j.bmc.2003.10.018
   PubMed Web of Science ®Google Scholar
• Ding, F., Han, B.-Y., Liu, W., Zhang, L., & Sun, Y. (2010). Interaction of imidacloprid with hemoglobin by fluorescence and circular dichroism. Journal of Fluorescence, 20, 753–762.10.1007/s10895-010-0618-0
   PubMed Web of Science ®Google Scholar
• Ding, F., Liu, W., Li, Y., Zhang, L., & Sun, Y. (2010). Determining the binding affinity and binding site of bensulfuron-methyl to human serum albumin by quenching of the intrinsic tryptophan fluorescence. Journal of Luminescence, 130, 2013–2021.10.1016/j.jlumin.2010.05.019
   Web of Science ®Google Scholar
• Ding, F., Liu, W., Liu, F., Li, Z.-Y., & Sun, Y. (2009). A study of the interaction between malachite green and lysozyme by steady-state fluorescence. Journal of Fluorescence, 19, 783–791.10.1007/s10895-009-0475-x
   PubMed Web of Science ®Google Scholar
• Ding, F., Liu, W., Zhang, L., Yin, B., & Sun, Y. (2010). Sulfometuron-methyl binding to human serum albumin: Evidence that sulfometuron-methyl binds at the Sudlow’s site I. Journal of Molecular Structure, 968, 59–66.10.1016/j.molstruc.2010.01.020
   Web of Science ®Google Scholar
• Garland, C. W. N., Joseph, W., & Shoemaker, D. P. (2003). Experiments in physical chemistry. New York, NY: McGraw-Hill.
   Google Scholar
• Ge, F., Chen, C., Liu, D., Han, B., Xiong, X., & Zhao, S. (2010). Study on the interaction between theasinesin and human serum albumin by fluorescence spectroscopy. Journal of Luminescence, 130, 168–173.10.1016/j.jlumin.2009.08.003
   Web of Science ®Google Scholar
• Greenfield, N. J., & Fasman, G. D. (1969). Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry, 8, 4108–4116.10.1021/bi00838a031
   PubMed Web of Science ®Google Scholar
• Hai, H., Miura, T., Kobayashi, T., Maéda, Y., & Miki, M. (2000). Conformational changes of the troponin – tropomyosin complex on F-actin observed by fluorescence resonance energy transfer measurements. Journal of Fluorescence, 10, 193–193.10.1023/A:1009455428604
   Web of Science ®Google Scholar
• Hamed-Akbari Tousi, S., Reza Saberi, M., & Chamani, J. (2010). Comparing the interaction of cyclophosphamide monohydrate to human serum albumin as opposed to holo-transferrin by spectroscopic and molecular modeling methods: Evidence for allocating the binding site. Protein and Peptide Letters, 17, 1524–1535.10.2174/0929866511009011524
   PubMed Web of Science ®Google Scholar
• He, Y., Wang, Y., Tang, L., Liu, H., Chen, W., Zheng, Z., & Zou, G. (2008). Binding of puerarin to human serum albumin: A spectroscopic analysis and molecular docking. Journal of Fluorescence, 18, 433–442.10.1007/s10895-007-0283-0
   PubMed Web of Science ®Google Scholar
• He, W., Li, Y., Tian, J., Liu, H., Hu, Z., & Chen, X. (2005). Spectroscopic studies on binding of shikonin to human serum albumin. Journal of Photochemistry and Photobiology A: Chemistry, 174, 53–61.10.1016/j.jphotochem.2005.03.016
   Web of Science ®Google Scholar
• Hink, M. A., Visser, N. V., Borst, J. W., van Hoek, A., & Visser, A. J. (2003). Practical use of corrected fluorescence excitation and emission spectra of fluorescent proteins in Förster resonance energy transfer (FRET) studies. Journal of Fluorescence, 13, 185–188.10.1023/A:1022947411788
   Web of Science ®Google Scholar
• Hurtado-Gómez, E., Barrera, F. N., & Neira, J. L. (2005). Structure and conformational stability of the enzyme I of Streptomyces coelicolor explored by FTIR and circular dichroism. Biophysical Chemistry, 115, 229–233.10.1016/j.bpc.2004.12.032
   PubMed Web of Science ®Google Scholar
• Iranfar, H., Rajabi, O., Salari, R., & Chamani, J. (2012). Probing the interaction of human serum albumin with ciprofloxacin in the presence of silver nanoparticles of three sizes: Multispectroscopic and ζ potential investigation. The Journal of Physical Chemistry B, 116, 1951–1964.10.1021/jp210685q
   PubMed Web of Science ®Google Scholar
• Kakehi, K., Oda, Y., & Kinoshita, M. (2001). Fluorescence polarization: Analysis of carbohydrate–protein interaction. Analytical Biochemistry, 297, 111–116.10.1006/abio.2001.5309
   PubMed Web of Science ®Google Scholar
• Kang, J., Liu, Y., Xie, M.-X., Li, S., Jiang, M., & Wang, Y.-D. (2004). Interactions of human serum albumin with chlorogenic acid and ferulic acid. Biochimica et Biophysica Acta (BBA)-General Subjects, 1674, 205–214.10.1016/j.bbagen.2004.06.021
   PubMed Web of Science ®Google Scholar
• Khan, S. N., Islam, B., Yennamalli, R., Zia, Q., Subbarao, N., & Khan, A. U. (2008). Characterization of doxorubicin binding site and drug induced alteration in the functionally important structural state of oxyhemoglobin. Journal of Pharmaceutical and Biomedical Analysis, 48, 1096–1104. doi:10.1016/j.jpba.2008.08.030
   PubMed Web of Science ®Google Scholar
• Khashi, M., Davoodnia, A., & Chamani, J. (2014). Dmap-catalyzed synthesis of novel pyrrolo[2,3-D]pyrimidine derivatives bearing an aromatic sulfonamide moiety. Phosphorus, Sulfur, and Silicon and the Related Elements, 189, 839–848.10.1080/10426507.2013.858253
   Web of Science ®Google Scholar
• Kristjánsdóttir, K. & Rudolph, J. (2003). A fluorescence polarization assay for native protein substrates of kinases. Analytical Biochemistry, 316, 41–49.10.1016/S0003-2697(03)00033-2
   PubMed Web of Science ®Google Scholar
• Li, Y., He, W., Dong, Y., Sheng, F., & Hu, Z. (2006). Human serum albumin interaction with formononetin studied using fluorescence anisotropy, FT-IR spectroscopy, and molecular modeling methods. Bioorganic & Medicinal Chemistry, 14, 1431–1436.10.1016/j.bmc.2005.09.066
   PubMed Web of Science ®Google Scholar
• Li, Y.-S., Ge, Y.-S., Zhang, Y., Zhang, A.-Q., Sun, S.-F., Jiang, F.-L., & Liu, Y. (2010). Interaction of coomassie brilliant blue G250 with human serum albumin: Probing of the binding mechanism and binding site by spectroscopic and molecular modeling methods. Journal of Molecular Structure, 968, 24–31.10.1016/j.molstruc.2010.01.015
   Web of Science ®Google Scholar
• Maciazek-Jurczyk, M., Sulkowska, A., Bojko, B., Rownicka-Zubik, J., & Sulkowski, W. W. (2009). Interaction of phenylbutazone and colchicine in binding to serum albumin in rheumatoid therapy: 1H NMR study. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 74, 1–9. doi:10.1016/j.saa.2009.06.043
   PubMed Web of Science ®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. doi:10.1016/j.jphotobiol.2010.02.009
   PubMed Web of Science ®Google Scholar
• Mansouri, M., Pirouzi, M., Saberi, M. R., Ghaderabad, M., & Chamani, J. (2013). Investigation on the interaction between cyclophosphamide and lysozyme in the presence of three different kind of cyclodextrins: Determination of the binding mechanism by spectroscopic and molecular modeling techniques. Molecules, 18, 789–813.10.3390/molecules18010789
   PubMed Web of Science ®Google Scholar
• Mirnezami, M., Restrepo, L., & Finch, J. (2003). Aggregation of sphalerite: role of zinc ions. Journal of Colloid and Interface Science, 259, 36–42.10.1016/S0021-9797(02)00101-7
   PubMed Web of Science ®Google Scholar
• Omidvar, Z., Parivar, K., Sanee, H., Amiri-Tehranizadeh, Z., Baratian, A., Saberi, M. R., … Chamani, J. (2011). Investigations with spectroscopy, zeta potential and molecular modeling of the non-cooperative behaviour between cyclophosphamide hydrochloride and aspirin upon interaction with human serum albumin: Binary and ternary systems from the view point of multi-drug therapy. Journal of Biomolecular Structure and Dynamics, 29, 181–206.10.1080/07391102.2011.10507382
   PubMed Web of Science ®Google Scholar
• Peng, J.-J., Liu, S.-P., Wang, L., & He, Y.-Q. (2010). Studying the interaction between CdTe quantum dots and Nile blue by absorption, fluorescence and resonance Rayleigh scattering spectra. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 75, 1571–1576.10.1016/j.saa.2010.02.021
   PubMed Web of Science ®Google Scholar
• Roessler, S., Zimmermann, R., Scharnweber, D., Werner, C., & Worch, H. (2002). Characterization of oxide layers on Ti6Al4V and titanium by streaming potential and streaming current measurements. Colloids and Surfaces B: Biointerfaces, 26, 387–395.10.1016/S0927-7765(02)00025-5
   Web of Science ®Google Scholar
• Sanei, H., Asoodeh, A., Hamedakbari-Tusi, S., & Chamani, J. (2011). Multi-spectroscopic investigations of aspirin and colchicine interactions with human hemoglobin: Binary and ternary systems. Journal of Solution Chemistry, 40, 1905–1931.10.1007/s10953-011-9766-3
   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. doi:10.1016/j.ijbiomac.2010.08.002
   PubMed Web of Science ®Google Scholar
• Spitz, J.-A., Polard, V., Maksimenko, A., Subra, F., Baratti-Elbaz, C., Méallet-Renault, R., … Auclair, C. (2007). Assessment of cellular actin dynamics by measurement of fluorescence anisotropy. Analytical Biochemistry, 367, 95–103.10.1016/j.ab.2007.04.001
   PubMed Web of Science ®Google Scholar
• Sun, H.-H., Zhang, J., Zhang, Y.-Z., Yang, L.-Y., Yuan, L.-L., & Liu, Y. (2012). Interaction of human serum albumin with 10-hydroxycamptothecin: spectroscopic and molecular modeling studies. Molecular Biology Reports, 39, 5115–5123.10.1007/s11033-011-1307-z
   PubMed Web of Science ®Google Scholar
• Vahedian-Movahed, H., Saberi, M., & Chamani, J. (2011). Comparison of binding interactions of lomefloxacin to serum albumin and serum transferrin by resonance light scattering and fluorescence quenching methods. Journal of Biomolecular Structure and Dynamics, 28, 483–502.10.1080/07391102.2011.10508590
   PubMed Web of Science ®Google Scholar
• Varlan, A. & Hillebrand, M. (2010). Bovine and human serum albumin interactions with 3-carboxyphenoxathiin studied by fluorescence and circular dichroism spectroscopy. Molecules, 15, 3905–3919.10.3390/molecules15063905
   PubMed Web of Science ®Google Scholar
• Vayá, I., Pérez-Ruiz, R., Lhiaubet-Vallet, V., Jiménez, M. C., & Miranda, M. A. (2010). Drug–protein interactions assessed by fluorescence measurements in the real complexes and in model dyads. Chemical Physics Letters, 486, 147–153.10.1016/j.cplett.2009.12.091
   Web of Science ®Google Scholar
• Wang, L., Chen, T., Qu, J., & Wei, X. (2010). Photobleaching-Based Quantitative Analysis of Fluorescence Resonance Energy Transfer inside Single Living Cell. Journal of Fluorescence, 20(1), 27–35.10.1007/s10895-009-0518-3
   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, 155–160.10.1016/j.saa.2010.03.006
   PubMed Web of Science ®Google Scholar
• Wang, Y.-Q., Zhang, H.-M., Zhang, G.-C., Zhou, Q.-H., Fei, Z.-H., Liu, Z.-T., & Li, Z.-X. (2008). Fluorescence spectroscopic investigation of the interaction between benzidine and bovine hemoglobin. Journal of Molecular Structure, 886, 77–84.10.1016/j.molstruc.2007.10.039
   Web of Science ®Google Scholar
• Wang, Y.-Q., Zhang, H.-M., Zhou, Q.-H., & Xu, H.-L. (2009). A study of the binding of colloidal Fe3O4 with bovine hemoglobin using optical spectroscopy. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 337, 102–108.
   Web of Science ®Google Scholar
• Wu, L., Mu, D., Gao, D., Deng, X., Tian, Y., Zhang, H., & Yu, A. (2009). Determination of protein by resonance light scattering technique using dithiothreitol–sodium dodecylbenzene sulphonate as probe. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 72, 178–181.10.1016/j.saa.2008.09.022
   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, 609–615.10.1016/j.jpba.2007.08.032
   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, 132–138.10.1016/j.molstruc.2007.09.002
   Web of Science ®Google Scholar
• Zhang, H.-M., Wang, Y.-Q., Zhou, Q.-H., & Wang, G.-L. (2009). Molecular interaction between phosphomolybdate acid and bovine hemoglobin. Journal of Molecular Structure, 921, 156–162.10.1016/j.molstruc.2008.12.049
   Web of Science ®Google Scholar
• Zhang, J., Sun, H.-H., Zhang, Y.-Z., Yang, L.-Y., Dai, J., & Liu, Y. (2012). Interaction of human serum albumin with indomethacin: Spectroscopic and molecular modeling studies. Journal of Solution Chemistry, 41, 422–435.10.1007/s10953-012-9809-4
   Web of Science ®Google Scholar
• Zhang, L.-N., Wu, F.-Y., & Liu, A.-H. (2011). Study of the interaction between 2, 5-di-[2-(4-hydroxy-phenyl) ethylene]-terephthalonitril and bovine serum albumin by fluorescence spectroscopy. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 79, 97–103.10.1016/j.saa.2011.02.013
   PubMed Web of Science ®Google Scholar
• Zhang, Y., Li, J.-H., Ge, Y.-S., Liu, X.-R., Jiang, F.-L., & Liu, Y. (2011). Biophysical studies on the interactions of a classic mitochondrial uncoupler with bovine serum albumin by spectroscopic, isothermal titration calorimetric and molecular modeling methods. Journal of Fluorescence, 21, 475–485.10.1007/s10895-010-0733-y
   PubMed Web of Science ®Google Scholar
• Zohoorian-Abootorabi, T., Sanee, H., Iranfar, H., Saberi, M. R., & Chamani, J. (2012). Separate and simultaneous binding effects through a non-cooperative behavior between cyclophosphamide hydrochloride and fluoxymesterone upon interaction with human serum albumin: Multi-spectroscopic and molecular modeling approaches. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 88, 177–191.10.1016/j.saa.2011.12.026
   PubMed Web of Science ®Google Scholar