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Research Articles

Acetaminophen interacts with human hemoglobin: optical, physical and molecular modeling studies

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Pages 1307-1321 | Received 18 Feb 2016, Accepted 15 Apr 2016, Published online: 20 May 2016

References

  • Abazari, O., Shafaei, Z., Divsalar, A., Eslami-Moghadam, M., Ghalandari, B., & Saboury, A. A. (2015). Probing the biological evaluations of a new designed pt(II) complex using spectroscopic & theoretical approaches: human hemoglobin as a target. Journal of Biomolecular Structure and Dynamics, 34, 1123–1131. doi:10.1080/07391102.2015.1071280
  • Abbasi-Tejarag, K., Divsalar, A., Saboury, A. A., Ghalandari, B., & Ghourchian, H. (2015). Destructive effect of anticancer oxali-palladium on heme degradation through the generation of endogenous hydrogen peroxide. Journal of Biomolecular Structure and Dynamics, Advance online publication.. doi:10.1080/07391102.2015.1121408
  • Abugo, O. O., & Rifkind, J. M. (1994). Oxidation of hemoglobin and the enhancement produced by nitroblue tetrazolium. The Journal of Biological Chemistry, 269, 24845–24853. Retrieved from http://www.jbc.org/content/269/40/24845.long
  • Anbazhagan, V., Sankhala, R. S., Singh, B. P., & Swamy, M. J. (2011). Isothermal titration calorimetric studies on the interaction of the major bovine seminal plasma protein, PDC-109 with phospholipid membranes. PLoS ONE, 6, 1–10. doi:10.1371/journal.pone.0025993
  • Bales, J. R., Nicholson, J. K., & Sadler, P. J. (1985). Two-dimensional proton nuclear magnetic resonance “maps” of acetaminophen metabolites in human urine. Clinical Chemistry, 31, 757–762. Retrieved from http://www.clinchem.org/content/31/5/757.full.pdf
  • 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. doi:10.1016/S0039-9140(00)00667-6
  • Basu, A., & Suresh Kumar, G. (2014). Interaction of the dietary pigment curcumin with hemoglobin: energetics of the complexation. Food & Function, 5, 1949–1955. doi:10.1039/c4fo00295d
  • Basu, A., & Suresh Kumar, G. (2015a). Interaction of toxic azo dyes with heme protein: Biophysical insights into the binding aspect of the food additive amaranth with human hemoglobin. Journal of Hazardous Materials, 289, 204–209. doi:10.1016/j.jhazmat.2015.02.044
  • Basu, A., & Suresh Kumar, G. (2015b). Binding of carmoisine, a food colorant, with hemoglobin: Spectroscopic and calorimetric studies. Food Research International, 72, 54–61. doi:10.1016/j.foodres.2015.03.015
  • Basu, A., & Suresh Kumar, G. (2015c). 199 Interaction of human hemoglobin with food colorants: a multifaceted biophysical study. Journal of Biomolecular Structure and Dynamics, 33, 131–132. doi:10.1080/07391102.2015.1032836
  • Bhattacharyya, J., Bhattacharyya, M., Chakraborti, A. S., & Poddar, R. K. (1998). Structural organisations of hemoglobin and myoglobin influence their binding behaviour with phenothiazines. International Journal of Biological Macromolecules, 23, 11–18. doi:10.1016/S0141-8130(98)00006-3
  • Buller, A., & Townsend, C. A. (2013). Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad. Proceedings of the National Academy of Sciences., 110, E653–E661. doi:10.1073/pnas.1221050110
  • Cheng, Y., Lin, H. K., Xue, D. P., Li, R Ch, & Wang, K. (2001). Lanthanide ions induce hydrolysis of hemoglobin-bound 2,3-diphosphoglycerate (2,3-DPG), conformational changes of globin and bidirectional changes of 2,3-DPG hemoglobin’s oxygen affinity. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1535, 200–216. doi:10.1016/S0925-4439(00)00100-9
  • Cheng, H., Liu, H., Bao, W., & Zou, G. (2011). Studies on the interaction between docetaxel and human hemoglobin by spectroscopic analysis and molecular docking. Journal of Photochemistry and Photobiology B: Biology, 105, 126–132. doi:10.1016/j.jphotobiol.2011.07.004
  • Dal Pan, G. J. (2013). Acetaminophen: Background and overview. U.S. Food and Drug Administration. Retrieved from http://www.fda.gov/downloads/Advisor.../UCM175767.pdf
  • Daneshgara, P., Moosavi-Movahedi, A. A., Norouzi, P., Ganjali, M. R., Madadkar Sobhani, A., & Saboury, A. A. (2009). Molecular interaction of human serum albumin with paracetamol: Spectroscopic and molecular modeling studies. International Journal of Biological Macromolecules, 45, 129–134. doi:10.1016/j.ijbiomac.2009.04.011
  • Das, A., & Suresh Kumar, G. (2016). Binding of the alkaloid aristololactam-β-D-glucoside and daunomycin to human hemoglobin: spectroscopy and calorimetry studies. Journal of Biomolecular Structure and Dynamics, 34, 800–813. doi:10.1080/07391102.2015.1055304
  • 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. doi:10.1007/s10895-009-0475-x
  • Dodson, G., & Wlodawer, A. (1998). Catalytic triads and their relatives. Trends in Biochemical Sciences, 23, 347–352. doi:10.1016/S0968-0004(98)01254-7
  • Elbum, D., & Nagel, R. (1981). Esterase Activity of Hemoglobin. Journal of Biological Chemistry, 256, 2280–2283. Retrieved from http://www.jbc.org/content/256/5/2280.full.pdf
  • Elmer, J., Harris, D. R., Sun, G., & Palmer, A. F. (2009). Purification of hemoglobin by tangential flow filtration with diafiltration. Biotechnology Progress, 25, 1402–1410. doi:10.1002/btpr.217
  • Fermi, G., Perutz, M. F., Shaanan, B., & Fourme, R. (1984). The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. Journal of Molecular Biology, 175, 159–174. doi:10.1016/0022-2836(84)90472-8
  • Fife, T. H. (1965). Steric effects in the hydrolysis of n-acylimidazoles and esters of p-nitrophenol. Journal of the American Chemical Society, 87, 4597–4600. doi:10.1021/ja00948a035
  • Flower, R. J., & Vane, J. R. (1972). Inhibition of prostaglandin synthetase in brain explains the anti-pyretic activity of paracetamol (4-acetamidophenol). Nature, 240, 410–411. doi:10.1038/240410a0
  • Forli, S., & Olson, A. J. (2012). A force field with discrete displaceable waters and desolvation entropy for hydrated ligand docking. Journal of Medicinal Chemistry, 55, 623–638. doi:10.1021/jm2005145
  • Freedman, R. B., & Radda, G. K. (1969). The interaction of 1-anilino-8-naphthalene sulphonate with erythrocyte membranes. FEBS Letters, 3, 150–152. doi:10.1016/0014-5793(69)80121-3
  • Gasteiger, J., & Marsili, M. (1980). Iterative partial equalization of orbital electronegativity—a rapid access to atomic charges. Tetrahedron, 36, 3219–3228. doi:10.1016/0040-4020(80)80168-2
  • Gaudreaua, S., Neaulta, J., Ramaswamy, F., Sarma, R. H., & Tajmir-Riahia, H. A. (2002). Interaction of AZT with human serum albumin studied by capillary electrophoresis, FTIR and CD spectroscopic methods. Journal of Biomolecular Structure and Dynamics, 19, 1007–1014. doi:10.1080/07391102.2002.10506804
  • Gebicka, L., & Banasiak, E. (2009). Flavonoids as reductants of ferryl hemoglobin. Acta Biochimica Polonica, 56, 509–513. Retrieved from http://www.actabp.pl/pdf/3_2009/509.pdf
  • Goyal, R. N., & Singh, S. P. (2006). Voltammetric determination of paracetamol at C60-modified glassy carbon electrode. Electrochimica Acta, 51, 3008–3012. doi:10.1016/j.electacta.2005.08.036
  • Harvey, J. W., French, T. W., & Senior, D. F. (1986). Hematological abnormalities associated with chronic acetaminophen administration in a dog. Journal of the American Veterinary Medical Association, 189, 1334–1335. Retrieved from http://europepmc.org/abstract/MED/3793579
  • Hazra, S., Hossain, M., & Suresh Kumar, G. (2013). Binding of isoquinoline alkaloids berberine, palmatine and coralyne to hemoglobin: structural and thermodynamic characterization studies. Molecular BioSystems, 9, 143–153. doi:10.1039/c2mb25345c.
  • Hazra, S., & Suresh Kumar, G. (2014). Structural and thermodynamic studies on the interaction of iminium and alkanolamine forms of sanguinarine with hemoglobin. The Journal of Physical Chemistry B, 118, 3771–3784. doi:10.1021/jp409764z.
  • Jasinska, A., Ferguson, A., Mohamed, W. S., & Szreder, T. (2009). The study of interactions between ibuprofen and bovine serum albumin. Food Chemistry and Biotechnology, 73, 15–24. Retrieved from http://repozytorium.p.lodz.pl/bitstream/handle/11652/245/The_study_of_interactions_Jasinska_2009.pdf?sequence=1
  • Lager, I., Looger, L. L., Hilpert, M., Lalonde, S., & Frommer, W. B. (2006). Conversion of a putative agrobacterium sugar-binding protein into a FRET sensor with high selectivity for sucrose. Journal of Biological Chemistry, 281, 30875–30883. doi:10.1074/jbc.M605257200
  • Lakowicz, J. R. (2006). Energy Transfer In: Principles of Fluorescence Spectroscopy. 3rd ed.. Springer, 443–472. Retrieved from http://www.springer.com/us/book/9780387312781
  • Lakowicz, J. R., & Weber, G. (1973). Quenching of fluorescence by oxygen, Probe for structural fluctuations in macromolecules. Biochemistry, 12, 4161–4170. doi:10.1021/bi00745a020
  • Leckband, D. (2000). Measuring the forces that control protein interactions. Annual Review of Biophysics and Biomolecular Structure, 29, 1–26. doi:10.1146/annurev.biophys.29.1.1
  • Lehrer, S. S. (1971). Solute perturbation of protein fluorescence. Quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry, 10, 3254–3263. doi:10.1021/bi00793a015.
  • Levy, A., Kuppusamy, P., & Rifkind, J. M. (1990). Multiple heme pocket subconformations of methemoglobin associated with distal histidine interactions. Biochemistry, 29, 9311–9316. doi:10.1021/bi00492a002
  • Lloyd, J. B. F. (1971). Synchronized excitation of fluorescence emission spectra. Nature Physical Science, 231, 64–65. doi:10.1038/physci231064a0
  • Lu, Z., Zhang, Y., Liu, H., Yuan, J., Zheng, Z., & Zou, G. (2007). Transport of a cancer chemopreventive polyphenol, resveratrol: Interaction with serum albumin and hemoglobin. Journal of Fluorescence, 17, 580–587. doi:10.1007/s10895-007-0220-2
  • MacNaughton, S. M. (2003). Acetaminophen toxicosis in a Dalmatian. Canadian Veterianary Journal, 44, 142–144. Retrieved from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC340050
  • 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. doi:10.1016/j.saa.2009.04.018.
  • Omotuyi, I. O., & Hamada, T. (2015). Dynamical footprint of falcipain-2 catalytic triad in hemoglobin-β-bound state. Journal of Biomolecular Structure and Dynamics, 33, 1027–1036. doi:10.1080/07391102.2014.924878
  • Perutz, M. F. (1970). Stereochemistry of cooperative effects in haemoglobin: Haem–haem interaction and the problem of allostery. Nature, 228, 726–734. doi:10.1038/228726a0.
  • Perutz, M. F., Fermi, G., Abraham, D. J., Poyart, C., & Bursaux, E. (1986). Hemoglobin as a receptor of drugs and peptides: x-ray studies of the stereochemistry of binding. Journal of the American Chemical Society, 108, 1064–1078. doi:10.1021/ja00265a036
  • Rashidipour, S., Naeeminejad, S., & Chamani, J. (2016). Study of the interaction between DNP and DIDS with human hemoglobin as binary and ternary systems: spectroscopic and molecular modeling investigation. Journal of Biomolecular Structure and Dynamics, 34, 57–77. doi:10.1080/07391102.2015.1009946
  • Ross, P. D., & Subramanian, S. (1981). Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry, 20, 3096–3102. doi:10.1021/bi00514a017
  • Roy, A., Sikdar, J., Seal, P., & Haldar, R. (2015). Cigarette smokers develop structurally modified hemoglobin: a possible way of increasing oxidative stress. Inhalation Toxicology, 27, 300–307. doi:10.3109/08958378.2015.1045052
  • Shaanan, B. (1983). Structure of human oxyhaemoglobin at 2·1resolution. Journal of Molecular Biology, 171, 31–59. doi:10.1016/S0022-2836(83)80313-1
  • Shahabadi, N., Maghsudi, M., Kiani, Z., & Pourfoulad, M. (2011). Multispectroscopic studies on the interaction of 2-tert-butylhydroquinone (TBHQ), a food additive, with bovine serum albumin. Food Chemistry, 124, 1063–1068. doi:10.1016/j.foodchem.2010.07.079
  • 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. doi:10.1016/j.jcis.2007.03.006
  • Solis, F. J., & Wets, R. J.-B. (1981). Minimization by random search technique. Mathematics of Operations Research, 6, 19–30. Retrieved from https://www.math.ucdavis.edu/~rjbw/mypage/Miscellaneous_files/randSearch.pdf
  • Stryer, L. (1965). The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. Journal of Molecular Biology, 13, 482–495. doi:10.1016/S0022-2836(65)80111-5.
  • Venkateshrao, S., & Manoharan, P. T. (2004). Conformational changes monitored by fluorescence study on reconstituted hemoglobins. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 60, 2523–2526. doi:10.1016/j.saa.2003.12.029.
  • Wallace, W. J., Maxwell, J. C., & Caughey, W. S. (1974). A role for chloride in the autoxidation of hemoglobin under conditions similar to those in erythrocytes. FEBS Letters, 43, 33–36. doi:10.1016/0014-5793(74)81099-9
  • 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. doi:10.1016/j.ijbiomac.2007.02.011
  • Wiseman, T., Williston, S., Brandts, J. F., & Lin, L. N. (1989). Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Analytical Biochemistry, 179, 131–137. doi:10.1016/0003-2697(89)90213-3
  • Yasmeen Khan, A., & Suresh Kumar, G. (2015). Natural isoquinoline alkaloids: binding aspects to functional proteins, serum albumins, hemoglobin, and lysozyme. Biophysical Reviews, 7, 407–420. doi:10.1007/s12551-015-0183-5.
  • Yuan, J. L., Liu, H., Kang, X., Lu, 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. doi:10.1016/j.molstruc.2008.04.017.
  • Zhang, Y., Li, Y., Dong, L., Li, J., He, W., Chen, X., & Hu, Z. (2008). Investigation of the interaction between naringin and human serum albumin. Journal of Molecular Structure, 875, 1–8. doi:10.1016/j.molstruc.2007.03.063.
  • Zhang, X., Li, L., Xu, Z., Liang, Z., Su, J., Huang, J., & Li, B. (2013). Investigation of the interaction of naringin palmitate with bovine serum albumin: Spectroscopic analysis and molecular docking. PLoS ONE, 8, 1–17. doi:10.1371/journal.pone.0059106.

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