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Research Articles

Characterization of the binding between anti-tumor drug 5-fluorouracil and human alpha-2-macroglobulin: spectroscopic and molecular docking analyses

, , ORCID Icon & ORCID Icon
Pages 7949-7959 | Received 18 Oct 2020, Accepted 15 Mar 2021, Published online: 02 Apr 2021

References

  • Abdi, K., Nafisi, S., Manouchehri, F., Bonsaii, M., & Khalaj, A. (2012). Interaction of 5-fluorouracil and its derivatives with bovine serum albumin. Journal of Photochemistry and Photobiology B, Biology, 107, 20–26. https://doi.org/10.1016/j.jphotobiol.2011.11.004
  • Ajmal, M. R., Nusrat, S., Alam, P., Zaidi, N., Khan, M. V., Zaman, M., Shahein, Y. E., Mahmoud, M. H., Badr, G., & Khan, R. H. (2017). Interaction of anticancer drug clofarabine with human serum albumin and human α-1 acid glycoprotein. Spectroscopic and molecular docking approach. Journal of Pharmaceutical and Biomedical Analysis, 135, 106–115. https://doi.org/10.1016/j.jpba.2016.12.001
  • Alam, P., Chaturvedi, S. K., Anwar, T., Siddiqi, M. K., Ajmal, M. R., Badr, G., Mahmoud, M. H., & Khan, R. H. (2015). Biophysical and molecular docking insight into the interaction of cytosine β-D arabinofuranoside with human serum albumin. Journal of Luminescence, 164, 123–130. https://doi.org/10.1016/j.jlumin.2015.03.011
  • Albani, J. R. (2011). Structure and dynamics of macromolecules: absorption and fluorescence studies. Elsevier.
  • Anand, U., Jash, C., Boddepalli, R. K., Shrivastava, A., & Mukherjee, S. (2011). Exploring the mechanism of fluorescence quenching in proteins induced by tetracycline. The Journal of Physical Chemistry B, 115(19), 6312–6320. https://doi.org/10.1021/jp2008978
  • Bakkialakshmi, S., & Chandrakala, D. (2011). A study on the interaction of 5-fluorouracil with human serum albumin using fluorescence quenching method. Journal of Pharmaceutical Sciences & Research, 3(7), 1326–1329.
  • Barrett, A. J., & Starkey, P. M. (1973). The interaction of alpha 2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism. The Biochemical Journal, 133(4), 709–724. https://doi.org/10.1042/bj1330709
  • BIOVIA. (2016). Discovery Studio 3.5 Modeling Environment, Release 2017. Dassault Systèmes.
  • Bodet, C. A., Jorgensen, J. H., & Drutz, D. J. (1985). Antibacterial activities of antineoplastic agents. Antimicrobial Agents and Chemotherapy, 28(3), 437–439. https://doi.org/10.1128/aac.28.3.437
  • Chinnathambi, S., Karthikeyan, S., Kesherwani, M., Velmurugan, D., & Hanagata, N. (2016). Underlying the mechanism of 5-fluorouracil and human serum albumin interaction: A biophysical study. Journal of Physical Chemsitry and Biophysics, 6, 214.
  • Chinnathambi, S., Velmurugan, D., Hanagata, N., Aruna, P. R., & Ganesan, S. (2014). Investigations on the interactions of 5-fluorouracil with bovine serum albumin: Optical spectroscopic and molecular modeling studies. Journal of Luminescence, 151, 1–10. https://doi.org/10.1016/j.jlumin.2014.01.063
  • Connors, K. (1987). Binding constants: The measurement of molecular complex stability. Wiley.
  • Desmond Molecular Dynamics System. (2013). Version 3.6, D. E. Shaw Research, Maestro-Desmond Interoperability Tools, version 3.6. Schrodinger.
  • Eftink, M. R. (1991). Fluorescence quenching reactions: Probing biological macro-molecular structures. In T. G. Dewey (Ed.), Biophysical and biochemical aspects of fluorescence spectroscopy (pp. 105–133). Plenum.
  • Eftink, M. R., & Ghiron, C. A. (1981). Fluorescence quenching studies with proteins. Analytical Biochemistry, 114(2), 199–227. https://doi.org/10.1016/0003-2697(81)90474-7
  • Ganrot, P. O. (1966). Determination of α2-macroglobulin as trypsin protein esterase. Clinica Chimica Acta, 14(4), 493–501. https://doi.org/10.1016/0009-8981(66)90037-4
  • Grem, J. L., Hoth, D. F., & Hamilton, J. M. (1986). Overview of current status and future direction of clinical trials with 5-fluorouracil in combination with folinic acid. Cancer Treatment Reviews, 71, 1249–1126.
  • Jorgensen, W. L., Maxwell, D. S., & Tirado-Rives, J. (1996). Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. Journal of the American Chemical Society, 118(45), 11225–11236. https://doi.org/10.1021/ja9621760
  • Jorgensen, W. L., & Tirado-Rives, J. (1988). The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin. Journal of the American Chemical Society, 110(6), 1657–1666. https://doi.org/10.1021/ja00214a001
  • Kasai, S., Horie, T., Mizuma, T., & Awazu, S. (1987). Fluorescence energy transfer study of the relationship between the lone tryptophan residue and drug binding sites in human serum albumin. Journal of Pharmaceutical Sciences, 76(5), 387–392. https://doi.org/10.1002/jps.2600760510
  • Kaur, I., & Katyal, A. (2011). Modification of mouse A2M B (620-792) and A2M N (168-230) by malondialdehyde and acetaldehyde attenuates the proteinase and TGF-β1 binding ability of A2MB. FEBS Letters, 585(6), 829–833. https://doi.org/10.1016/j.febslet.2011.02.008
  • Kuzmanic, B., & Zagrovic, B. (2010). Determination of ensemble-average pairwise root mean-square deviation from experimental B-factors. Biophysical Journal, 98(5), 861–871. https://doi.org/10.1016/j.bpj.2009.11.011
  • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680–685. https://doi.org/10.1038/227680a0
  • Lakowicz, J. R. (1999). Introduction to fluorescence. In Principles of Fluorescence Spectroscopy (pp. 1–23). Springer.
  • Marrero, A., Duquerroy, S., Trapani, S., Goulas, T., Guevara, T., Andersen, G. R., Navaza, J., Sottrup-Jensen, L., & Gomis-Rüth, F. X. (2012). The crystal structure of human α2-macroglobulin reveals a unique molecular cage. Angewandte Chemie (International ed. in English), 51(14), 3340–3344. https://doi.org/10.1002/anie.201108015
  • Morris, S. M. (1993). The genetic toxicology of 5-fluoropyrimidines and 5-chlorouracil. Mutation Research, 297(1), 39–51. https://doi.org/10.1016/0165-1110(93)90006-9
  • Noordhuis, P., Holwerda, U., Van der Wilt, C. L., Van Groeningen, C. J., Smid, K., Meijer, S., Pinedo, H. M., & Peters, G. J. (2004). 5-Fluorouracil incorporation into RNA and DNA in relation to thymidylate synthase inhibition of human colorectal cancers. Annals of Oncology: Official Journal of the European Society for Medical Oncology, 15(7), 1025–1032. https://doi.org/10.1093/annonc/mdh264
  • Nyhlen, A., Ljungberg, B., Nilsson-Ehle, I., & Odenholt, I. (2002). Bactericidal effect of combinations of antibiotic and antineoplastic agents against Staphylococcus aureus and Escherichia coli. Chemotherapy, 48(2), 71–77. https://doi.org/10.1159/000057665
  • Perez-Iratxeta, C., & Andrade-Navarro, M. A. (2008). K2D2: Estimation of protein secondary structure from circular dichroism spectra. BMC Structural Biology, 8, 25–25. https://doi.org/10.1186/1472-6807-8-25
  • Peters, G. J., Laurensse, E., Leyva, A., Lankelma, J., & Pinedo, H. M. (1986). Sensitivity of human, murine, and rat cells to 5-fluorouracil and 50-deoxy-5-fluorouridine in relation to drug metabolizing enzymes. Cancer Research, 46, 20–28.
  • Rabbani, G., Khan, M. J., Ahmad, A., Maskat, M. Y., & Khan, R. H. (2014). Effect of copper oxide nanoparticles on the conformation and activity of β–galactosidase. Colloids and Surfaces B: Biointerfaces, 123, 96–105. https://doi.org/10.1016/j.colsurfb.2014.08.035
  • Rehman, A. A., Ahsan, H., & Khan, F. H. (2013). α-2-macroglobulin: A physiological guardian. Journal of Cellular Physiology, 228(8), 1665–1675. Aughttps://doi.org/10.1002/jcp.24266
  • Ross, P. D., & Rekharsky, M. V. (1996). Thermodynamics of hydrogen bond and hydrophobic interactions in cyclodextrin complexes. Biophysical Journal, 71(4), 2144–2154. https://doi.org/10.1016/S0006-3495(96)79415-8
  • Ross, P. D., & Subramanian, S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20(11), 3096–3102. https://doi.org/10.1021/bi00514a017
  • Shivakumar, D., Williams, J., Wu, Y., Damm, W., Shelley, J., & Sherman, W. (2010). Prediction of absolute solvation free energies using molecular dynamics free energy perturbation and the OPLS force field. Journal of Chemical Theory and Computation, 6(5), 1509–1519. https://doi.org/10.1021/ct900587b
  • Siddiqui, T., Zia, M. K., Ahsan, H., & Khan, F. H. (2020). Quercetin-induced inactivation and conformational alterations of alpha-2-macroglobulin: Multi-spectroscopic and calorimetric study. Journal of Biomolecular Structure & Dynamics, 38(14), 4107–4112. https://doi.org/10.1080/07391102.2019.1671232
  • Siddiqui, T., Zia, M. K., Ali, S. S., Ahsan, H., & Khan, F. H. (2018). Insight into the interactions of proteinase inhibitor- alpha-2-macroglobulin with hypochlorite. International Journal of Biological Macromolecules, 117, 401–406. https://doi.org/10.1016/j.ijbiomac.2018.05.112
  • Siddiqui, T., Zia, M. K., Ali, S. S., Ahsan, H., & Khan, F. H. (2019). Inactivation of alpha-2-macroglobulin by photoilluminated gallic acid. Journal of Fluorescence, 29(4), 969–911. https://doi.org/10.1007/s10895-019-02410-3
  • Siddiqui, T., Zia, M. K., Ali, S. S., Rehman, A. A., Ahsan, H., & Khan, F. H. (2016). Reactive oxygen species and anti-proteinases. Archives of Physiology and Biochemistry, 122(1), 1–7. https://doi.org/10.3109/13813455.2015.1115525
  • Siddiqui, T., Zia, M. K., Ali, S. S., Rehman, A. A., Ahsan, H., & Khan, F. H. (2019). Investigating hydrogen peroxide induced damage to alpha-2-macroglobulin: Biophysical and thermodynamic study. Journal of Molecular Structure, 1195, 904–913. https://doi.org/10.1016/j.molstruc.2019.06.017
  • Sottrup-Jensen, L. (1989). α-macroglobulins: Structure, shape, and mechanism of proteinase complex formation. Journal of Biological Chemistry, 264(20), 11539–11543. https://doi.org/10.1016/S0021-9258(18)80094-1
  • Tian, J. N., Liu, J. Q., He, W. Y., Hu, Z. D., Yao, X. J., & Chen, X. G. (2004). Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method. Biomacromolecules, 5(5), 1956–1961. https://doi.org/10.1021/bm049668m
  • Tian, W., Chen, C., Lei, X., Zhao, J., & Liang, J. (2018). CASTp 3.0: Computed atlas of surface topography of proteins. Nucleic Acids Research, 46(W1), W363–W367. https://doi.org/10.1093/nar/gky473
  • Wallace, A. C., Laskowski, R. A., & Thornton, J. M. (1995). LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Engineering, 8(2), 127–134. https://doi.org/10.1093/protein/8.2.127
  • Wang, X. Y., Lin, J., Zhang, X. M., Liu, Q., Xu, Q., Tan, R. X., & Guo, Z. J. (2003). 5-Fluorouracilcisplatin adducts with potential antitumor activity. Journal of Inorganic Biochemistry, 94(12), 186–192. https://doi.org/10.1016/S0162-0134(02)00618-9
  • Yuan, L., Liu, M., Sun, B., Liu, J., Wei, X., Wang, Z., Wang, B., & Han, J. (2017). Calorimetric and spectroscopic studies on the competitive behavior between (−)-epigallocatechin-3-gallate and 5-fluorouracil with human serum albumin. Journal of Molecular Liquids, 248, 330–339. https://doi.org/10.1016/j.molliq.2017.10.049
  • Zhang, X., Li, L., Xu, Z., Su, J., Li, B., & Huang, J. (2014). Studies on the interaction of naringin palmitate with lysozyme by spectroscopic analysis. Journal of Functional Foods, 8, 331–339. https://doi.org/10.1016/j.jff.2014.03.026
  • Zia, M. K., Siddiqui, T., Ahsan, H., & Khan, F. H. (2020). Comprehensive insight into the molecular interaction of an anticancer drug-ifosfamide with human alpha-2-macroglobulin: biophysical and in silico studies. Journal of Biomolecular Structure & Dynamics, 1–10. 10.1080/07391102.2020.1852115 33267704
  • Zia, M. K., Siddiqui, T., Ali, S. S., Ahsan, H., & Khan, F. H. (2018a). Interaction of anti-cancer drug-cisplatin with major proteinase inhibitor-alpha-2-macroglobulin: Biophysical and thermodynamic analysis. International Journal of Biological Macromolecules, 116, 721–727. https://doi.org/10.1016/j.ijbiomac.2018.05.041
  • Zia, M. K., Siddiqui, T., Ali, S. S., Ahsan, H., & Khan, F. H. (2018b). Exploring the interaction of anti-androgen drug-bicalutamide with human alpha-2-macroglobulin: A Biophysical investigation. International Journal of Biological Macromolecules, 120(Pt B), 2285–2292. https://doi.org/10.1016/j.ijbiomac.2018.08.117
  • Zia, M. K., Siddiqui, T., Ali, S. S., Ahsan, H., & Khan, F. H. (2019a). Understanding the binding interaction between methotrexate and human alpha-2-macroglobulin: Multi-spectroscopic and computational investigation. Archives of Biochemistry and Biophysics, 675, 108118. https://doi.org/10.1016/j.abb.2019.108118
  • Zia, M. K., Siddiqui, T., Ali, S. S., Ahsan, H., & Khan, F. H. (2019b). Deciphering the binding of dutasteride with human alpha-2-macroglobulin: Molecular docking and calorimetric approach. International Journal of Biological Macromolecules, 133, 1081–1089. https://doi.org/10.1016/j.ijbiomac.2019.04.180
  • Zolotnitsky, G., Cogan, U., Adir, N., Solomon, V., Shoham, G., & Shoham, Y. (2004). Mapping glycoside hydrolase substrate subsites by isothermal titration calorimetry. Proceedings of the National Academy of Sciences of the United States of America, 101(31), 11275–11280. https://doi.org/10.1073/pnas.0404311101

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