Detection of interaction between ornidazole and albumin by using thermodynamic parameters

  • Authors

    • Esra MaltaÅŸ Çağıl Selcuk University, Faculty of Pharmacy, Selcuklu, Konya, Turkey
    2021-11-04
    https://doi.org/10.14419/ijac.v9i2.31798
  • Ornidazole, Human Serum Albumin (HSA), Fluorescence Quenching, Stern Volmer Equation, Thermodynamic Parameter.
  • The binding of 1-chloro-3-(2-methyl-5-nitro-1H-imidazole-1-yl) propan-2-ol (Ornidazole) to human serum albumin (HSA) was studied by fluorescence and UV-visible spectroscopy. Interaction of ornidazole (OR) with HSA was identified by Stern-Volmer and Van’t Hoff equations. The binding constant, Kb and the thermodynamic parameters, ∆H, ∆S, and ∆G at different temperatures were calculated by several equations. Data shows that the fluorescence quenching mechanism of HSA with ornidazole may occur via static quenching. The thermodynamic parameters showed that van der Waals interactions and hydrogen bonds are the major forces for the interaction of ornidazole with HSA. The spectral changes of synchronous fluorescence suggested that both the microenvironment of OR and the conformation of HSA concerning their concentrations have changed during binding.

     

     

     

  • References

    1. [1] Luo, H., Du, Y., Guo, ZX. (2009). Electrochemistry of N-n-undecyl-N′-(sodium-p aminobenzenesulfonate) thiourea and its interaction with bovine serum albumin. Bioelectrochemistry, 4: 232–235. https://doi.org/10.1016/j.bioelechem.2008.10.004.

      [2] Banerjee, M., Pal, U., Subudhhi, A., Chakrabarti, A., Basu, S. (2012). Interaction of Merocyanine 540 with serum albumins: photophysical and binding studies. Journal of Photochemistry Photobiology B Biology, 108: 23–33. https://doi.org/10.1016/j.jphotobiol.2011.12.005.

      [3] He, X.M., Carter, D.C. (1992). Atomic structure and chemistry of human serum albumin. Nature, 358: 209–215. https://doi.org/10.1038/358209a0.

      [4] Sevilla, P., Rivas, J.M., García-Blanco, F., García-Ramos, J.V., Sánchez-Corté, S. (2007). Identification of the antitumoral drug emodin binding sites in bovine serum albumin by spectroscopic methods. Biochimica Biophysica Acta, 1774: 1359–1369. https://doi.org/10.1016/j.bbapap.2007.07.022.

      [5] Carter, D., Ho, J.X. (1994). In Advances in Protein Chemistry (Anfinsen CB, Edsall JT, Richards FM, and Eisenberg DS, eds.), vol. 45, Academic Press, New York: 153–203.

      [6] Peters, T. Advances in Protein Chemistry. vol. 37, Academic Press, New York: 161–245 (a); Tayeh N, Rungassamy T, Albani JR. 2009. J Pharmaceutical Biomedical Analysis 1985, 50: 107–116 (b). https://doi.org/10.1016/j.jpba.2009.03.015.

      [7] Tsujino, I., Anderson, G.S., Sieber, F. (2001). Postirradiation hyperthermia selectively potentiates the merocyanine 540-sensitized photoinactivation of small cell lung cancer cells. Photochemistry Photobiology, 73: 191–198. https://doi.org/10.1562/0031-8655(2001)073<0191:PHSPTM>2.0.CO;2.

      [8] Ghoneim, M.M., El-Desoky, H.S., Abdel-Galeil, M.M. (2011). Electrochemistry of the antibacterial and antifungal drug nitroxoline and its determination in bulk form, pharmaceutical formulation and human blood. Bioelectrochemistry, 80:162–168. https://doi.org/10.1016/j.bioelechem.2010.08.003.

      [9] Fotouhi L, Banafsheh S, Heravi MM. (2009). Electrochemistry of the interaction of furazolidone and bovine serum albumin. Bioelectrochemistry, 77: 26–30. https://doi.org/10.1016/j.bioelechem.2009.05.011.

      [10] Otto, J., Lesko, L.J. (1986). Protein binding of nifedipine. Journal of Pharmacy Pharmacology, 38(5): 399-400. https://doi.org/10.1111/j.2042-7158.1986.tb04598.x.

      [11] Guo, Q.L., Li, R., Zhou, X., Liu, Y. (2008). Study on the interaction of ketoconazole with human and bovine serum albumins by fluorescence spectroscopy. Chinese Journal of Chemistry, 26(12): 2207-2215. https://doi.org/10.1002/cjoc.200890393.

      [12] Zhang, Q., Nia, Y., Kokot, S. (2012). Combined voltammetric and spectroscopic analysis of small molecule-biopolymer interactions: The levodopa and serum albumin system. Talanta, 15(88): 524-532. https://doi.org/10.1016/j.talanta.2011.11.027.

      [13] Ravera, M., Gabano, E., Baracco, S., Osella, D. (2009). Electrochemical evaluation of the interaction between antitumoral titanocene dichloride and biomolecules. Inorganica Chimica Acta, 362: 1303–1306. https://doi.org/10.1016/j.ica.2008.06.022.

      [14] Nayar, S., Mir, A., Ashok, A., Guha, A. and Sharma, V. (2010). Bovine Serum Albumin Binding and Drug Delivery Studies with PVA-Ferrofluid. Journal of Bionic Engineering, 7: 29–34. https://doi.org/10.1016/S1672-6529(09)60188-8.

      [15] Bi, S., Sun, Y., Qiao, C., Zhang, H., Liu, C.(2009). Binding of several anti-tumor drugs to bovine serum albumin: Fluorescence study. Journal of Luminescence, 129: 541–547. https://doi.org/10.1016/j.jlumin.2008.12.010.

      [16] 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. https://doi.org/10.1016/j.molstruc.2004.11.062.

      [17] Erkkola, R., Järvinen, H. (1987). Single dose of ornidazole in the treatment of bacterial vaginosis. Annales Chirurgiae et Gynaecologiae, 202: 94-96.

      [18] Pradeep, A.R., Kalra, N., Priyanka, N., Naik, S.B. (2012). Microbiological outcomes of systemic ornidazole use in chronic periodontitis. Part II Journal of the International Academy of Periodontology, 14(2): 50-54.

      [19] Grewal, A.S., Bhardwaj, S.K., Patro, S.K., Kanungo, S.K. (2012). Visible spectrophotometric estimation of ornidazole in pure and pharmaceutical formulation. International Journal of Chemical Technology Research, 4(3): 1044-1048.

      [20] Asane, G.S., Rao, Y.M., Bhatt, J.H., Shaikh, K.S. (2011). Optimization, characterisation and pharmacokinetic studies of mucoadhesive oral multiple unit systems of ornidazole. Scientia Pharmaceutica, 79(1): 181-196. https://doi.org/10.3797/scipharm.1003-03.

      [21] Wei, T.-T., Sun, J.-H., Han L.-W., Chen K., Wang Z.-Q., Ji, H. (2015). Effects of the ornidazole enantiomers on the central nervous system: Involvement of the GABAA receptor, Chemical Biology Interactions, 5(242): 163-9 https://doi.org/10.1016/j.cbi.2015.09.019.

      [22] 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 79: 97–103. https://doi.org/10.1016/j.saa.2011.02.013.

      [23] Lakowicz, J.R. (2006). Principles of Fluorescence Spectroscopy, third ed, Springer press, New York https://doi.org/10.1007/978-0-387-46312-4.

      [24] Yang, J., Jing, Z.H., Jie, J.J., Guo, P. (2009). Fluorescence spectroscopy study on the interaction between Gossypol and bovine serum albumin. Journal of Molecular Structures, 920: 227–230. https://doi.org/10.1016/j.molstruc.2008.10.053.

      [25] Han, X.L., Mei, P., Liu, Y., Xiao, Q., Jiang, F.L., Li, R. (2009). Binding interaction of quinclorac with bovine serum albumin: A biophysical study. Spectrochimica Acta A, 74: 781–787. https://doi.org/10.1016/j.saa.2009.08.018.

      [26] Li, Y., Yang, G.Z., Mei, Z. (2012). Spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albumin. Acta Pharmaceutica Sinica B, 2(1): 53–59. https://doi.org/10.1016/j.apsb.2011.12.001.

      [27] Zhang, G., Chen, X., Guo, J., Wang, J. (2009). Spectroscopic investigation of the interaction between chrysin and bovine serum albumin. Journal of Molecular Structures, 921: 346–51. https://doi.org/10.1016/j.molstruc.2009.01.036.

      [28] Tong, J.Q., Zhang, H.X., Yang, H.M., Mei, P. (2010). Photochemical studies on the binding of an organic fluoride to bovine serum albumin. Molecular Biology Reports, 37: 1741–1747. https://doi.org/10.1007/s11033-009-9598-z.

      [29] Yu, J.H., Li, B., Dai, P., Ge, S.G. (2009). Molecular simulation of the interaction between novel type rhodanine derivative probe and bovine serum albumin. Spectrochimica Acta A, 74: 277–281. https://doi.org/10.1016/j.saa.2009.06.013.

      [30] Maltas, E. (2014). Interactions of nicleasmide with serum proteins. Journal of Food Drug Analysis, 22: 549-555. https://doi.org/10.1016/j.jfda.2014.03.004.

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    Maltaş Çağıl, E. (2021). Detection of interaction between ornidazole and albumin by using thermodynamic parameters. International Journal of Advanced Chemistry, 9(2), 161-167. https://doi.org/10.14419/ijac.v9i2.31798