Investigation of binding properties of two ethidium derivatives with serum albumins: spectral and computational approach

References

• Abdelhameed, A. S., Alam, P., & Khan, R. H. (2015). Binding of janus kinase ınhibitor tofacitinib with human serum albumin: Multi-technique approach. Journal of Biomolecular Structure and Dynamics, 34, 2037–2044. doi:10.1080/07391102.2015.1104522
   Web of Science ®Google Scholar
• Akbay, N., Seferoğlu, Z., & Gök, E. (2009). Fluorescence interaction and determination of calf thymus DNA with two ethidium derivatives. Journal of Fluorescence, 19, 1045–1051.10.1007/s10895-009-0504-9
   PubMed Web of Science ®Google Scholar
• Ariga, G. G., Naik, P. N., Nandibewoor, S. T., & Chimatadar, S. A. (2016). Quenching of fluorescence by meclizine, a probe study for structural and conformational changes in human serum albümin. Journal of Biomolecular Structure and Dynamics, 1–15. doi:10.1080/07391102.2016.1245159
   PubMed Web of Science ®Google Scholar
• Babu, E., Mareeswaran, P. M., Singaravadivel, S., Bhuvaneswari, J., & Rajagopal, S. (2014). A selective, long-lived deep-red emissive ruthenium(II) polypyridine complexes for the detection of BSA. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 130, 553–560.10.1016/j.saa.2014.04.060
   PubMed Web of Science ®Google Scholar
• Bi, S., Yan, L., Sun, Y., & Zhang, H. (2011). Investigation of ketoprofen binding to human serum albumin by spectral methods. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 78, 410–414.10.1016/j.saa.2010.11.002
   PubMed Web of Science ®Google Scholar
• Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., & Karplus, M. (1983). CHARMM: A program for macromolecular energy, minimization, and dynamics calculations. Journal of Computational Chemistry, 4, 187–217.10.1002/(ISSN)1096-987X
   Web of Science ®Google Scholar
• Bujacz, A. (2012). Structures of bovine, equine and leporine serum albumin. Acta Crystallographica Section D: Biological Crystallography, D68, 1278–1289.
   Google Scholar
• Dassault Systèmes BIOVIA (2016). Discovery studio modeling environment. San Diego: Dassault Système.
   Google Scholar
• Gelamo, E. L., Silva, C. H. T. P., Imasato, H., & Tabak, M. (2002). Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: Spectroscopy and modelling. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1594, 84–99.10.1016/S0167-4838(01)00287-4
   PubMed Web of Science ®Google Scholar
• Guo, X., Han, X., & Tong, J. (2010). The investigation of the interaction between piracetam and bovine serum albumin by spectroscopic methods. Journal of Molecular Structure, 966, 129–135.10.1016/j.molstruc.2009.12.025
   Web of Science ®Google Scholar
• Hao, A., Guo, X., Wu, Q., Sun, Y., Cong, C., & Liu, W. (2016). Exploring the interactions between polyethyleneimine modified fluorescent carbon dots and bovine serum albumin by spectroscopic methods. Journal of Luminescence, 170, 90–96.10.1016/j.jlumin.2015.10.002
   Web of Science ®Google Scholar
• Hu, Y. J., Liu, Y., Shen, X. S., Fang, X. Y., & Qu, S. S. (2005). Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin. Journal of Molecular Structure, 738, 143–147.10.1016/j.molstruc.2004.11.062
   Web of Science ®Google Scholar
• Jafari, F., Samadi, S., Nowroozi, A., Sadrjavadi, K., Moradi, S., Ashrafi-Kooshk, M. R., & Shahlaei, M. (2017). Experimental and computational studies on the binding of diazinon to human serum albumin. Journal of Biomolecular Structure and Dynamics, 1–21. doi:10.1080/07391102.2017.1329096
   PubMed Web of Science ®Google Scholar
• Johnson, I. M., Kumar, S. G., & Malathi, R. (2003). De-intercalation of ethidium bromide and acridine orange by xanthine derivatives and their modulatory effect on anticancer agents: A study of DNA-directed toxicity enlightened by time correlated single photon counting. Journal of Biomolecular Structure and Dynamics., 20, 677–685.10.1080/07391102.2003.10506884
   PubMed Web of Science ®Google Scholar
• Kabir, Md. Zahirul, Feroz, S. R., Mukarram, A. K., Alias, Z., Mohamad, S. B., & Tayyab, S. (2016). Interaction of a tyrosine kinase inhibitor, vandetanib with human serum albumin as studied by fluorescence quenching and molecular docking. Journal of Biomolecular Structure and Dynamics., 34, 1693–1704.10.1080/07391102.2015.1089187
   PubMed Web of Science ®Google Scholar
• Larsericsdotter, H., Oscarsson, S., & Buijs, J. (2005). Structure, stability, and orientation of BSA adsorbed to silica. Journal of Colloid and Interface Science, 289, 26–35.10.1016/j.jcis.2005.03.064
   PubMed Web of Science ®Google Scholar
• Liu, J., Yue, Y., Wang, J., Yan, X., Liu, R., Sun, Y., & Li, X. (2015). Study of interaction between human serum albumin and three phenanthridine derivatives: Fluorescence spectroscopy and computational approach. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 145, 473–481.
   PubMed Web of Science ®Google Scholar
• Luedtke, N. W., Liu, Q., & Tor, Y. (2003). Synthesis, photophysical properties, and nucleic acid binding of phenanthridinium derivatives based on ethidium. Bioorganic & Medicinal Chemistry, 11, 5235–5247.10.1016/j.bmc.2003.08.006
   PubMed Web of Science ®Google Scholar
• N’ soukpoé-Kossi, C. N., St-Louis, C., Beauregard, M., Subirade, M., Carpentier, R., Hotchandani, S. & Tajmir-Riahi, H. A. (2006). Resveratrol binding to human serum albumin. Journal of Biomolecular Structure and Dynamics., 24, 277–283.
   PubMed Web of Science ®Google Scholar
• Naik, P. N., Chimatadar, S. A., & Nandibewoor, S. T. (2009). Study on the interaction between antibacterial drug and bovine serum albumin: A spectroscopic approach. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 73, 841–845.10.1016/j.saa.2009.04.018
   PubMed Web of Science ®Google Scholar
• Nishiwaki, H., Miura, M., Imai, K., Ohno, R., Kawashima, K., Ezaki, K., … Yamada, K. (1974). Experimental studies on the antitumor effect of ethidium bromide and related substances. Cancer Research., 34, 2699–2703.
   PubMed Web of Science ®Google Scholar
• Ross, P. D., & Subramanian, S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20, 3096–3102.10.1021/bi00514a017
   PubMed Web of Science ®Google Scholar
• Salci, A., & Toprak, M. (2017). Spectroscopic investigations on the binding of Pyronin Y to human serum albümin. Journal of Biomolecular Structure and Dynamics., 35, 8–16.10.1080/07391102.2015.1128357
   PubMed Web of Science ®Google Scholar
• Shahabadi, N., Hadidi, S., & Feizi, F. (2015). Study on the interaction of antiviral drug ‘Tenofovir’ with human serum albumin by spectral and molecular modeling methods. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 138, 169–175.10.1016/j.saa.2014.10.070
   PubMed Web of Science ®Google Scholar
• Shang, L., Jiang, X., & Dong, S. (2006). In vitro study on the binding of neutral red to bovine serum albumin by molecular spectroscopy. Journal of Photochemistry and Photobiology A: Chemistry, 184, 93–97.10.1016/j.jphotochem.2006.04.003
   Web of Science ®Google Scholar
• Singh, N., Pagariya, D., Jain, S., Naik, S., & Kishore, N. (2017). Interaction of copper (II) complexes by bovine serum albumin: Spectroscopic and calorimetric insights. Journal of Biomolecular Structure and Dynamics, 1–14. doi:10.1080/07391102.2017.1355848
   PubMed Web of Science ®Google Scholar
• Sun, Y., Bi, S., Song, D., Qiao, C., Mu, D., & Zhang, H. (2008). Study on the interaction mechanism between DNA and the main active components in Scutellaria baicalensis Georgi. Sensors and Actuators B: Chemical, 129, 799–810.10.1016/j.snb.2007.09.082
   PubMed Web of Science ®Google Scholar
• Wang, Y. Q., Zhang, H. M., & Zhang, G. C. (2006). Studies of the interaction between palmatine hydrochloride and human serum albumin by fluorescence quenching method. Journal of Pharmaceutical and Biomedical Analysis, 41, 1041–1046.10.1016/j.jpba.2006.01.028
   PubMed Web of Science ®Google Scholar
• Wei, Y., Li, J., Dong, C., Shuang, S., Liu, D., & Huie, C. (2006). Investigation of the association behaviors between biliverdin and bovine serum albumin by fluorescence spectroscopy. Talanta, 70, 377–382.10.1016/j.talanta.2006.02.052
   PubMed Web of Science ®Google Scholar
• Wu, G., Robertson, D. H., Brooks, C. L., & Vieth, M. (2003). Detailed analysis of grid-based molecular docking: A case study of CDOCKER-A CHARMm-based MD docking algorithm. Journal of Computational Chemistry, 24, 1549–1562.10.1002/(ISSN)1096-987X
   PubMed Web of Science ®Google Scholar
• Yue, Y., Liu, J., Liu, R., Dong, Q., & Fan, J. (2014a). Binding of helicid to human serum albumin: A hybrid spectroscopic approach and conformational study. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 124, 46–51.
   PubMed Web of Science ®Google Scholar
• Yue, Y., Liu, J., Liu, R., Sun, Y., Li, X., & Fan, J. (2014b). The binding affinity of phthalate plasticizers-protein revealed by spectroscopic techniques and molecular modeling. Food and Chemical Toxicology., 71, 244–253.10.1016/j.fct.2014.06.022
   PubMed Web of Science ®Google Scholar
• Yue, Y., Dong, Q., Zhang, Y., Li, X., Yan, X., Sun, Y., & Liu, J. (2016a). Synthesis of imidazole derivatives and the spectral characterization of the binding properties towards human serum albümin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 153, 688–703.
   PubMed Web of Science ®Google Scholar
• Yue, Y., Sun, Y., Yan, X., Liu, J., Zhao, S., & Zhang, J. (2016b). Evaluation of the binding of perfluorinated compound to pepsin: Spectroscopic analysis and molecular docking. Chemosphere, 161, 475–481.10.1016/j.chemosphere.2016.07.047
   PubMed Web of Science ®Google Scholar
• Yue, Y., Zhao, S., Sun, Y., Yan, X., Liu, J., & Zhang, J. (2017). Effects of plant extract aurantio-obtusin on pepsin structure: Spectroscopic characterization and docking simulation. Journal of Luminescence., 187, 333–339.10.1016/j.jlumin.2017.03.041
   Web of Science ®Google Scholar
• Zhang, L. L., Ma, F. F., Kuang, Y. F., Cheng, S., Long, Y. F., & Xiao, Q. G. (2016). Highly sensitive detection of bovine serum albumin based on the aggregation of triangular silver nanoplates. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 154, 98–102.10.1016/j.saa.2015.10.019
   PubMed Web of Science ®Google Scholar
• Zhou, X. M., Yang, Q., Xie, X. Y., Hu, Q., Qi, F. M., Rahman, Z. U., & Chen, X. G. (2012). NMR, multi-spectroscopic and molecular modeling approach to investigate the complexes between C.I. Acid Orange 7 and human serum albumin in vitro. Dyes and Pigments, 92, 1100–1107.10.1016/j.dyepig.2011.08.012
   Web of Science ®Google Scholar
• Zhou, H., Shi, X., Fan, Y., He, Z., Gu, W., Ye, L., & Meng, F. (2017). Interaction of Prussian blue nanoparticles with bovine serum albumin: A multi- spectroscopic approach. Journal of Biomolecular Structure and Dynamics, 1–8. doi:10.1080/07391102.2016.1274273
   Web of Science ®Google Scholar