Electrochemical and in Silico Investigations of the Interaction between Nitro Blue Tetrazolium Chloride and Bovine Serum Albumin

Dilek  Kazıcı; Mehmet Abdullah  Alagöz; Ebru Kuyumcu  Savan

doi:10.37819/nanofab.007.225

Electrochemical and in Silico Investigations of the Interaction between Nitro Blue Tetrazolium Chloride and Bovine Serum Albumin

Dilek Kazıcı

Mehmet Abdullah Alagöz

Ebru Kuyumcu Savan

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Abstract

The binding ability of the drug on its interaction with the protein will also significantly affect the apparent volume of distribution of the drugs and, in many cases the rate of elimination of the drugs. The interactions of proteins and other molecules are a fascinating topic applied to surface technologies and sensors. Therefore, it is aimed to determine the NBTCand to elucidate its interaction with Bovine Serum Albumin (BSA) by electrochemical and in silico studies in this paper. The reduction in BSA oxidation signals measured by differential pulse voltammetry upon incubation with different NBTC concentrations indicated that NBTC was bound to BSA. In addition, in silico (molecular modeling and molecular dynamics) studies have been conducted on the interactions of NBTC with proteins in plasma. As a result of the in silico studies investigated the interactions of NBTC with serum albumin, its binding affinity, and the dynamic process in the binding state. In silico studies showed that NBTC binds to BSA with high affinity (with -7.986 kcal/mol docking score), and this binding was stable (with a 3.0 average RMSD value). Eventually, the results of the electrochemical and modeling studies were perfectly matched.

Keywords: Nitro Blue Tetrazolium Chloride Bovine Serum Albumin in Silico Voltammetry

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References

Al-Otaibi, J. S., Mary, Y. S., Mary, Y. S., & Aayisha, S. (2022). Polycyclic Aromatic Compounds, https://doi.org/10.1080/10406638.2022.2032765.
Baehner, R. L, & Nathan, D. G. (1968). Quantitative Nitroblue Tetrazolium Test in Chronic Granulomatous Disease. The New England Journal of Medicine, 278, 971-976. doi: 10.1056/NEJM19680502278180.
Baehner, R. L., & Johnston, R. B. (1972). Monocyte Function in Children With Neutropenia and Chronic Infections. Blood, 40, 31–41. https://doi.org/10.1182/blood.V40.1.31.31.
Baehner, R. L., Boxer, L. A., & Davis, J. (1976). The biochemical basis of nitroblue tetrazolium reduction in normal human and chronic granulomatous disease polymorphonuclear leukocytes. Blood, 48, 309-313. https://doi.org/10.1182/blood.V48.2.309.309.
Chen, N., Di, P., Ning, S., Jiang, W., Jing, Q., Ren, G., Liu, Y., Tang, Y., Xu, Z., Liu, G., & Ren. F. (2019). Modified rivaroxaban microparticles for solid state properties improvement based on drug-protein/polymer supramolecular interactions. Powder Technology, 344, 819-829. https://doi.org/10.1016/j.powtec.2018.12.085.
Gosser, D. K. (1993). Cyclic Voltammetry; Simulation and Analysis of Reaction Mechanisms. Synthesis and Reactivity in Inorganic and Metal-Organic Chemistry, 24, 1237–1238. doi:10.1080/00945719408001398.
Hanımeli, Ö. A., Yılmaz, Ö., & Yüksel, H. (2010). Primer immün yetmezlikli çocuğa yaklaşım. Dicle Medical Journal, 37(3), 307-313. https://dergipark.org.tr/en/pub/dicletip/issue/4697/64071.
Jalali, F., & Dorraji, P. S. (2012). Electrochemical and spectroscopic studies of the interaction between the neuroleptic drug, gabapentin, and DNA. Journal of Pharmaceutical and Biomedical Analysis, 70, 598–601. doi:10.1016/j.jpba.2012.06.005.
Kato, S., Kikuchi, R., Aoshima, H., Saitoh, Y., & Miwa, N. (2010). Defensive effects of fullerene-C60/liposome complex against UVA-induced intracellular reactive oxygen species generation and cell death in human skin keratinocytes HaCaT, associated with intracellular uptake and extracellular excretion of fullerene-C60. Journal of Photochemistry and Photobiology B: Biology, 98(2), 144-151. https://doi.org/10.1016/j.jphotobiol.2009.11.015
Kragh-Hansen, U., Chaung, V. T. G., & Otagiri, M. (2002). Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biological and Pharmaceutical Bulletin, 25, 695–704. https://doi.org/10.1248/bpb.25.695.
Kuzu, B., Hepokur, C.., Alagoz, M. A., Burmaoglu, S., & Algul, O. (2022). Synthesis, Biological Evaluation and In Silico Studies of Some 2-Substituted Benzoxazole Derivatives as Potential Anticancer Agents to Breast Cancer. Chemistry Select. 7, e202103559. https://doi.org/10.1002/slct.202103559.
Laviron, E. (1979). General expression of the linear potential sweep voltammogram in the case of diffusionless electrochemical systems. Journal of Electroanalytical Chemistry and Interfacial Electrochemistry, 101, 19–28. https://doi.org/10.1016/S0022-0728(79)80075-3
Müller, W. E., & Wollert, U. (1979). Human serum albumin as a ‘silent receptor’ for drugs and endogenous substances. Pharmacology 19, 59–67. https://doi.org/10.1159/000137289.
Naggar, A.H., Kaoutit, M.E., Naranjo-Rodriguez, I., El-Sayed, A.Y., & Cisneros, J.L.H.H. (2016). Voltammetric and Spectroscopic Investigation of the Interaction Between 1,4-Benzodiazepines and Bovine Serum Albumin. Journal of Solution Chemistry, 45, 1659–1678. https://doi.org/10.1007/s10953-016-0532-4.
Oritani, T., Fukuhara, N., Okajima, T., Kitamura, F., Ohsaka, T., & Oritani, T. (2004). Electrochemical and spectroscopic studies on electron-transfer reaction between novel water-soluble tetrazolium salts and a superoxide ion. Inorganica Chimica Acta, 357, 436–442. https://doi.org/10.1016/j.ica.2003.05.007.
Ozten, O., Zengin Kurt, B., Sonmez, F., Dogan, B., & Durdagi, S. (2021). Synthesis, molecular docking and molecular dynamics studies of novel tacrine-carbamate derivatives as potent cholinesterase inhibitors. Bioorganic Chemistry 115, 105225. https://doi.org/10.1016/j.bioorg.2021.105225.
Priel, D. L., & Kuhns, D. B. 5th (Ed.) (2019). Assessment of neutrophil function. eds. Clinical Immunology: Principles and Practice (chap 94). Philadelphia, USA: Elsevier.
Seydel, J. K., & Schaper, K. J. (1982). Quantitative structure-pharmacokinetic relationships and drug design. Pharmacology & Therapeutics, 15, 131–182. https://doi.org/10.1016/0163-7258(81)90040-1.
Soares, S., Mateus, N., & Freitas, V. D. (2007). Interaction of different polyphenols with bovine serum albumin (BSA) and human salivary alpha-amylase (HSA) by fluorescence quenching. Journal of Agricultural and Food Chemistry, 55, 6726–6735. https://doi.org/10.1021/jf070905x.
Tian, J. N., Xie, Y. H., Zhao, Y. C., Li, C. F., & Zhao, S. L. (2011). Spectroscopy characterization of the interaction between brevifolin carboxylic acid and bovine serum albümin. Luminescence, 26, 296–304. https://doi.org/10.1002/bio.1227.

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Electrochemical and in Silico Investigations of the Interaction between Nitro Blue Tetrazolium Chloride and Bovine Serum Albumin. (2022). Nanofabrication, 7, 40-51. https://doi.org/10.37819/nanofab.007.225

How to Cite

Electrochemical and in Silico Investigations of the Interaction between Nitro Blue Tetrazolium Chloride and Bovine Serum Albumin. (2022). Nanofabrication, 7, 40-51. https://doi.org/10.37819/nanofab.007.225

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Dilek Kazıcı

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Mehmet Abdullah Alagöz

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Ebru Kuyumcu Savan

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[1] Al-Otaibi, J. S., Mary, Y. S., Mary, Y. S., & Aayisha, S. (2022). Polycyclic Aromatic Compounds, https://doi.org/10.1080/10406638.2022.2032765.

[2] Baehner, R. L, & Nathan, D. G. (1968). Quantitative Nitroblue Tetrazolium Test in Chronic Granulomatous Disease. The New England Journal of Medicine, 278, 971-976. doi: 10.1056/NEJM19680502278180.

[3] Baehner, R. L., & Johnston, R. B. (1972). Monocyte Function in Children With Neutropenia and Chronic Infections. Blood, 40, 31–41. https://doi.org/10.1182/blood.V40.1.31.31.

[4] Baehner, R. L., Boxer, L. A., & Davis, J. (1976). The biochemical basis of nitroblue tetrazolium reduction in normal human and chronic granulomatous disease polymorphonuclear leukocytes. Blood, 48, 309-313. https://doi.org/10.1182/blood.V48.2.309.309.

[5] Chen, N., Di, P., Ning, S., Jiang, W., Jing, Q., Ren, G., Liu, Y., Tang, Y., Xu, Z., Liu, G., & Ren. F. (2019). Modified rivaroxaban microparticles for solid state properties improvement based on drug-protein/polymer supramolecular interactions. Powder Technology, 344, 819-829. https://doi.org/10.1016/j.powtec.2018.12.085.

[6] Gosser, D. K. (1993). Cyclic Voltammetry; Simulation and Analysis of Reaction Mechanisms. Synthesis and Reactivity in Inorganic and Metal-Organic Chemistry, 24, 1237–1238. doi:10.1080/00945719408001398.

[7] Hanımeli, Ö. A., Yılmaz, Ö., & Yüksel, H. (2010). Primer immün yetmezlikli çocuğa yaklaşım. Dicle Medical Journal, 37(3), 307-313. https://dergipark.org.tr/en/pub/dicletip/issue/4697/64071.

[8] Jalali, F., & Dorraji, P. S. (2012). Electrochemical and spectroscopic studies of the interaction between the neuroleptic drug, gabapentin, and DNA. Journal of Pharmaceutical and Biomedical Analysis, 70, 598–601. doi:10.1016/j.jpba.2012.06.005.

[9] Kato, S., Kikuchi, R., Aoshima, H., Saitoh, Y., & Miwa, N. (2010). Defensive effects of fullerene-C60/liposome complex against UVA-induced intracellular reactive oxygen species generation and cell death in human skin keratinocytes HaCaT, associated with intracellular uptake and extracellular excretion of fullerene-C60. Journal of Photochemistry and Photobiology B: Biology, 98(2), 144-151. https://doi.org/10.1016/j.jphotobiol.2009.11.015

[10] Kragh-Hansen, U., Chaung, V. T. G., & Otagiri, M. (2002). Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biological and Pharmaceutical Bulletin, 25, 695–704. https://doi.org/10.1248/bpb.25.695.

[11] Kuzu, B., Hepokur, C.., Alagoz, M. A., Burmaoglu, S., & Algul, O. (2022). Synthesis, Biological Evaluation and In Silico Studies of Some 2-Substituted Benzoxazole Derivatives as Potential Anticancer Agents to Breast Cancer. Chemistry Select. 7, e202103559. https://doi.org/10.1002/slct.202103559.

[12] Laviron, E. (1979). General expression of the linear potential sweep voltammogram in the case of diffusionless electrochemical systems. Journal of Electroanalytical Chemistry and Interfacial Electrochemistry, 101, 19–28. https://doi.org/10.1016/S0022-0728(79)80075-3

[13] Müller, W. E., & Wollert, U. (1979). Human serum albumin as a ‘silent receptor’ for drugs and endogenous substances. Pharmacology 19, 59–67. https://doi.org/10.1159/000137289.

[14] Naggar, A.H., Kaoutit, M.E., Naranjo-Rodriguez, I., El-Sayed, A.Y., & Cisneros, J.L.H.H. (2016). Voltammetric and Spectroscopic Investigation of the Interaction Between 1,4-Benzodiazepines and Bovine Serum Albumin. Journal of Solution Chemistry, 45, 1659–1678. https://doi.org/10.1007/s10953-016-0532-4.

[15] Oritani, T., Fukuhara, N., Okajima, T., Kitamura, F., Ohsaka, T., & Oritani, T. (2004). Electrochemical and spectroscopic studies on electron-transfer reaction between novel water-soluble tetrazolium salts and a superoxide ion. Inorganica Chimica Acta, 357, 436–442. https://doi.org/10.1016/j.ica.2003.05.007.

[16] Ozten, O., Zengin Kurt, B., Sonmez, F., Dogan, B., & Durdagi, S. (2021). Synthesis, molecular docking and molecular dynamics studies of novel tacrine-carbamate derivatives as potent cholinesterase inhibitors. Bioorganic Chemistry 115, 105225. https://doi.org/10.1016/j.bioorg.2021.105225.

[17] Priel, D. L., & Kuhns, D. B. 5th (Ed.) (2019). Assessment of neutrophil function. eds. Clinical Immunology: Principles and Practice (chap 94). Philadelphia, USA: Elsevier.

[18] Seydel, J. K., & Schaper, K. J. (1982). Quantitative structure-pharmacokinetic relationships and drug design. Pharmacology & Therapeutics, 15, 131–182. https://doi.org/10.1016/0163-7258(81)90040-1.

[19] Soares, S., Mateus, N., & Freitas, V. D. (2007). Interaction of different polyphenols with bovine serum albumin (BSA) and human salivary alpha-amylase (HSA) by fluorescence quenching. Journal of Agricultural and Food Chemistry, 55, 6726–6735. https://doi.org/10.1021/jf070905x.

[20] Tian, J. N., Xie, Y. H., Zhao, Y. C., Li, C. F., & Zhao, S. L. (2011). Spectroscopy characterization of the interaction between brevifolin carboxylic acid and bovine serum albümin. Luminescence, 26, 296–304. https://doi.org/10.1002/bio.1227.