Structural dynamics studies on the binding of aflatoxin B₁ to chicken egg albumin using spectroscopic techniques and molecular docking

References

• Abdin, M. Z., Ahmad, M. M., & Javed, S. (2010). Advances in molecular detection of Aspergillus: An update. Archives of Microbiology, 192(6), 409–425. doi: 10.1007/s00203-010-0563-y
   PubMed Web of Science ®Google Scholar
• Afrin, S., Rahman, Y., & Tabish, M. (2019). Elucidating the interaction of ticlopidine with serum albumin and its role in bilirubin displacement in vitro. Journal of Biomolecular Structure and Dynamics, 37(4), 863–876. doi: 10.1080/07391102.2018.1449667
   PubMed Web of Science ®Google Scholar
• Ahmad, M., Ahmad, M. M., Hamid, R., Abdin, M. Z., & Javed, S. (2013). Use of response surface methodology to study the effect of media composition on aflatoxin production by Aspergillus flavus. Mycotoxin Research, 29(1), 39–45. doi: 10.1007/s12550-012-0151-x
   PubMed Web of Science ®Google Scholar
• Ahmed, A., Shamsi, A., Khan, M. S., Husain, F. M., & Bano, B. (2018). Methylglyoxal induced glycation and aggregation of human serum albumin: Biochemical and biophysical approach. International Journal of Biological Macromolecules, 113, 269–276. doi: 10.1016/j.ijbiomac.2018.02.137
   PubMed Web of Science ®Google Scholar
• Bagheri, M., & Fatemi, M. H. (2018). Fluorescence spectroscopy, molecular docking and molecular dynamic simulation studies of HSA-aflatoxin B1 and G1 interactions. Journal of Luminescence, 202, 345–353. doi: 10.1016/j.jlumin.2018.05.066
   Web of Science ®Google Scholar
• Bhogale, A., Patel, N., Mariam, J., Dongre, P. M., Miotello, A., & Kothari, D. C. (2014). Comprehensive studies on the interaction of copper nanoparticles with bovine serum albumin using various spectroscopies. Colloids and Surfaces B: Biointerfaces, 113, 276–284. doi: 10.1016/j.colsurfb.2013.09.021
   PubMed Web of Science ®Google Scholar
• Bhogale, A., Patel, N., Sarpotdar, P., Mariam, J., Dongre, P. M., Miotello, A., & Kothari, D. C. (2013). Systematic investigation on the interaction of bovine serum albumin with ZnO nanoparticles using fluorescence spectroscopy. Colloids and Surfaces B: Biointerfaces, 102, 257–264. doi: 10.1016/j.colsurfb.2012.08.023
   PubMed Web of Science ®Google Scholar
• Burstein, E. A., Vedenkina, N. S., & Ivkova, M. N. (1973). Fluorescence and the location of tryptophan residues in protein molecules. Photochemistry and Photobiology, 18(4), 263–279. doi: 10.1111/j.1751-1097.1973.tb06422.x
   PubMed Web of Science ®Google Scholar
• Chaturvedi, S. K., Ahmad, E., Khan, J. M., Alam, P., Ishtikhar, M., & Khan, R. H. (2015). Elucidating the interaction of limonene with bovine serum albumin: A multi-technique approach. Molecular Biosystems, 11(1), 307–316. doi: 10.1039/C4MB00548A
   PubMed Web of Science ®Google Scholar
• Clarke, D. T. (2012). Circular dichroism in protein folding studies. In Mark L. Chiu, John E. Coligan, Mohamed Abdel-Mohsen, David W. Speicher, & Paul T. Wingfield (Eds.), Current Protocols in Protein Science (Vol. 70, pp. 28.3.1–28.3.17). Hoboken, NJ: John Wiley & Sons. doi: 10.1002/0471140864.ps2803s70
   Google Scholar
• Corcuera, L.-A., Ibáñez-Vea, M., Vettorazzi, A., González-Peñas, E., & Cerain, A. L. D. (2011). Validation of a UHPLC-FLD analytical method for the simultaneous quantification of aflatoxin B1 and ochratoxin a in rat plasma, liver and kidney. Journal of Chromatography B, 879(26), 2733–2740. doi: 10.1016/j.jchromb.2011.07.039
   PubMed Web of Science ®Google Scholar
• Coulombe, R. A., Shelton, D. W., Sinnhuber, R. O., & Nixon, J. E. (1982). Comparative mutagenicity of aflatoxins using a Salmonella/trout hepatic enzyme activation system. Carcinogenesis, 3(11), 1261–1264. doi: 10.1093/carcin/3.11.1261
   PubMed Web of Science ®Google Scholar
• Cunningham, L. W., Clouse, R. W., & Ford, J. D. (1963). Heterogeneity of the carbohydrate moiety of crystalline ovalbumin. Biochimica et Biophysica Acta, 78(2), 379–381. doi: 10.1016/0006-3002(63)91652-4
   PubMedGoogle Scholar
• Dantas, M. D. A., Tenório, H. A., Lopes, T. I. B., Pereira, H. J. V., Marsaioli, A. J., Figueiredo, I. M., & Antos, J. C. C. (2017). Interactions of tetracyclines with ovalbumin, the main allergen protein from egg white: Spectroscopic and electrophoretic studies. International Journal of Biological Macromolecules, 102, 505–514. doi: 10.1016/j.ijbiomac.2017.04.052
   PubMed Web of Science ®Google Scholar
• Dirr, H. W., & Schabort, J. C. (1986). Aflatoxin B1 transport in rat blood plasma. Binding to albumin in vivo and in vitro and spectrofluorimetric studies into the nature of the interaction. Biochimica et Biophysica Acta (BBA) - General Subjects, 881(3), 383–390. doi: 10.1016/0304-4165(86)90030-9
   PubMedGoogle Scholar
• Faisal, Z., Lemli, B., Szerencsés, D., Kunsági-Máté, S., Bálint, M., Hetényi, C., … Poór, M. (2018). Interactions of zearalenone and its reduced metabolites α-zearalenol and β-zearalenol with serum albumins: Species differences, binding sites, and thermodynamics. Mycotoxin Research, 34(4), 269–278. doi: 10.1007/s12550-018-0321-6
   PubMed Web of Science ®Google Scholar
• Frisvad, J. C., & Samson, R. A. (2004). Emericella venezuelensis, a new species with stellate ascospores producing sterigmatocystin and aflatoxin B1. Systematic and Applied Microbiology, 27(6), 672–680. doi: 10.1078/0723202042369910
   PubMed Web of Science ®Google Scholar
• Golli-Bennour, E. E., Kouidhi, B., Bouslimi, A., Abid-Essefi, S., Hassen, W., & Bacha, H. (2010). Cytotoxicity and genotoxicity induced by aflatoxin B1, ochratoxin A, and their combination in cultured Vero cells. Journal of Biochemical and Molecular Toxicology, 24(1), 42–50. doi: 10.1002/jbt.20310
   PubMed Web of Science ®Google Scholar
• Goux, W. J., & Venkatasubramanian, P. N. (1986). Metal ion binding properties of hen ovalbumin and S-ovalbumin: Characterization of the metal ion binding site by 31P NMR and water proton relaxation rate enhancements. Biochemistry, (1983), 84–94. doi: 10.1021/bi00349a013
   Google Scholar
• Hanwell, M. D., Curtis, D. E., Lonie, D. C., Vandermeersch, T., Zurek, E., & Hutchison, G. R. (2012). Avogadro: An advanced semantic chemical editor, visualization, and analysis platform. Journal of Cheminformatics, 4(1), 17. doi: 10.1186/1758-2946-4-17
   PubMed Web of Science ®Google Scholar
• Hu, Y.-J., Liu, Y., Wang, J.-B., Xiao, X.-H., & Qu, S.-S. (2004). Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin. Journal of Pharmaceutical and Biomedical Analysis, 36(4), 915–919. doi: 10.1016/j.jpba.2004.08.021
   PubMed Web of Science ®Google Scholar
• Ikhlas, S., Usman, A., & Ahmad, M. (2019). Comparative study of the interactions between bisphenol-A and its endocrine disrupting analogues with bovine serum albumin using multi-spectroscopic and molecular docking studies. Journal of Biomolecular Structure and Dynamics, 37(6), 1427–1437. doi: 10.1080/07391102.2018.1461136
   PubMed Web of Science ®Google Scholar
• Ishtikhar, M., Khan, S., Badr, G., Osama Mohamed, A., & Khan, R. H. (2014). Interaction of the 5-fluorouracil analog 5-fluoro-2’-deoxyuridine with “N” and “B” isoforms of human serum albumin: A spectroscopic and calorimetric study. Molecular BioSystems, 10(11), 2954–2964. doi: 10.1039/C4MB00306C
   PubMed Web of Science ®Google Scholar
• Kandagal, P. B., Ashoka, S., Seetharamappa, J., Shaikh, S. M. T., Jadegoud, Y., & Ijare, O. B. (2006). Study of the interaction of an anticancer drug with human and bovine serum albumin: Spectroscopic approach. Journal of Pharmaceutical and Biomedical Analysis, 41(2), 393–399. doi: 10.1016/j.jpba.2005.11.037
   PubMed Web of Science ®Google Scholar
• Kathiravan, A., Paramaguru, G., & Renganathan, R. (2009). Study on the binding of colloidal zinc oxide nanoparticles with bovine serum albumin. Journal of Molecular Structure, 934(1–3), 129–137. doi: 10.1016/j.molstruc.2009.06.032
   Web of Science ®Google Scholar
• Khalid, M., Siddiqui, T., Saqib, S., Ahsan, H., & Halim, F. (2018). Exploring the interaction of anti-androgen drug-bicalutamide with human alpha-2-macroglobulin: A biophysical investigation. International Journal of Biological Macromolecules, 120, 2285–2292. doi: 10.1016/j.ijbiomac.2018.08.117
   PubMed Web of Science ®Google Scholar
• Lakowicz, J. R. (2006). Principles of fluorescence spectroscopy. US: Springer. doi: 10.1007/978-0-387-46312-4
   Google Scholar
• Li, X., & Yan, Y. (2017). Comparative study of the interactions between ovalbumin and five antioxidants by spectroscopic methods. Journal of Fluorescence, 27(1), 213–225. doi: 10.1007/s10895-016-1948-3
   PubMed Web of Science ®Google Scholar
• Ma, Z., Prasanna, G., Jiang, L., & Jing, P. (2019). Molecular interaction of cyanidin-3-O-glucoside with ovalbumin: Insights from spectroscopic, molecular docking, and in vitro digestive studies. Journal of Biomolecular Structure and Dynamics, 1102, 1–17. doi: 10.1080/07391102.2019.1618735
   Google Scholar
• Mansouri, A., Mousavi, M., Attar, F., Akbar, A., & Falahati, M. (2018). Interaction of manganese nanoparticle with cytochrome c: A multi-spectroscopic study. International Journal of Biological Macromolecules, 106, 78–86. doi: 10.1016/j.ijbiomac.2017.07.175
   PubMed Web of Science ®Google Scholar
• McReynolds, L., O’Malley, B. W., Nisbet, A. D., Fothergill, J. E., Givol, D., Fields, S., … Brownlee, G. G. (1978). Sequence of chicken ovalbumin mRNA. Nature, 273(5665), 723–728. doi: 10.1038/273723a0
   PubMed Web of Science ®Google Scholar
• Miller, J. N., Miller, J., Miller, J. N., Miller, J. M., Miller, J., & Miller, J.-A. (1979). Recent advances in molecular luminescence analysis. Retrieved from https://www.scienceopen.com/document?vid=8cccd245-7752-4971-a886-dd9c2f067da1
   Google Scholar
• Mishra, H. N., & Das, C. (2003). A review on biological control and metabolism of aflatoxin. Critical Reviews in Food Science and Nutrition, 43(3), 245–264. doi: 10.1080/10408690390826518
   PubMed Web of Science ®Google Scholar
• Morris, G. M., Huey, R., Lindstrom, W., Sanner, M. F., Belew, R. K., Goodsell, D. S., & Olson, A. J. (2009). AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. Journal of Computational Chemistry, 30(16), 2785–2791. doi: 10.1002/jcc.21256
   PubMed Web of Science ®Google Scholar
• Ognjenović, J., Stojadinović, M., Milčić, M., Apostolović, D., Vesić, J., Stambolić, I., … Velickovic, T. C. (2014). Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white. Food Chemistry, 164, 36–43. doi: 10.1016/j.foodchem.2014.05.005
   PubMed Web of Science ®Google Scholar
• Pathak, M., Mishra, R., Agarwala, P. K., Ojha, H., Singh, B., Singh, A., & Kukreti, S. (2016). Binding of ethyl pyruvate to bovine serum albumin: Calorimetric, spectroscopic and molecular docking studies. Thermochimica Acta, 633(633), 140–148. doi: 10.1016/j.tca.2016.04.006
   Google Scholar
• Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004). UCSF Chimera—A visualization system for exploratory research and analysis. Journal of Computational Chemistry, 25(13), 1605–1612. doi: 10.1002/jcc.20084
   PubMed Web of Science ®Google Scholar
• Poór, M., Bálint, M., Hetényi, C., Gődér, B., Kunsági-Máté, S., Kőszegi, T., & Lemli, B. (2017). Investigation of non-covalent interactions of aflatoxins (B1, B2, G1, G2, and M1) with serum albumin. Toxins, 9(11), 339. doi: 10.3390/toxins9110339
   Web of Science ®Google Scholar
• Rajaian, H., Symonds, H. W., & Bowmer, C. J. (1997). Drug binding sites on chicken albumin: A comparison to human albumin. Journal of Veterinary Pharmacology and Therapeutics, 20(6), 421–426. doi: 10.1046/j.1365-2885.1997.00099.x
   PubMed Web of Science ®Google Scholar
• Richard, J. L. (2008). Discovery of aflatoxins and significant historical features. Toxin Reviews, 27(3–4), 171–201. doi: 10.1080/15569540802462040
   Web of Science ®Google Scholar
• Ross, P. D., & Subramanian, S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20(11), 3096–3102. doi: 10.1021/bi00514a017
   PubMed Web of Science ®Google Scholar
• Sabbioni, G., Ambs, S., Wogan, G. N., & Groopman, J. D. (1990). The aflatoxin-lysine adduct quantified by high-performance liquid chromatography from human serum albumin samples. Carcinogenesis, 11(11), 2063–2066. doi: 10.1093/carcin/11.11.2063
   PubMed Web of Science ®Google Scholar
• Scholl, P. F., Turner, P. C., Sutcliffe, A. E., Sylla, A., Diallo, M. S., Friesen, M. D., … Wild, C. P. (2006). Quantitative comparison of aflatoxin B1 serum albumin adducts in humans by isotope dilution mass spectrometry and ELISA. Cancer Epidemiology Biomarkers & Prevention, 15(4), 823–826. doi: 10.1158/1055-9965.EPI-05-0890
   PubMed Web of Science ®Google Scholar
• Selva Sharma, A., Anandakumar, S., & Ilanchelian, M. (2014). A combined spectroscopic and molecular docking study on site selective binding interaction of toluidine blue O with human and bovine serum albumins. Journal of Luminescence, 151, 206–218. doi: 10.1016/j.jlumin.2014.02.009
   Web of Science ®Google Scholar
• Siddiqi, M. K., Alam, P., Chaturvedi, S. K., Nusrat, S., Ajmal, M. R., Abdelhameed, A. S., & Khan, R. H. (2017). Probing the interaction of cephalosporin antibiotic-ceftazidime with human serum albumin: A biophysical investigation. International Journal of Biological Macromolecules, 105(Pt 1), 292–299. doi: 10.1016/j.ijbiomac.2017.07.036
   PubMedGoogle Scholar
• Siddiqui, G. A., Siddiqi, M. K., Khan, R. H., & Naeem, A. (2018). Probing the binding of phenolic aldehyde vanillin with bovine serum albumin: Evidence from spectroscopic and docking approach. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 203, 40–47. doi: 10.1016/j.saa.2018.05.023
   PubMed Web of Science ®Google Scholar
• Stein, P. E., Leslie, A. G., Finch, J. T., & Carrell, R. W. (1991). Crystal structure of uncleaved ovalbumin at 1.95 Å resolution. Journal of Molecular Biology, 221(3), 941–959. doi: 10.1016/0022-2836(91)80185-W
   PubMed Web of Science ®Google Scholar
• Stein, P. E., Leslie, A. G., Finch, J. T., Turnell, W. G., McLaughlin, P. J., & Carrell, R. W. (1990). Crystal structure of ovalbumin as a model for the reactive centre of serpins. Nature, 347(6288), 99–102. doi: 10.1038/347099a0
   PubMed Web of Science ®Google Scholar
• Sudlow, G., Birkett, D. J., & Wade, D. N. (1975). The characterization of two specific drug binding sites on human serum albumin. Molecular Pharmacology, 11(6), 824–832. PMID 1207674
   PubMed Web of Science ®Google Scholar
• Tan, H., Chen, L., Ma, L., Liu, S., Zhou, H., Zhang, Y., … Yu, Y. (2019). Fluorescence spectroscopic investigation of competitive interactions between quercetin and aflatoxin B1 for binding to human serum albumin. Toxins, 11(4), 214. doi: 10.3390/toxins11040214
   Web of Science ®Google Scholar
• Valeur, B., & Brochon, J.-C. (2001). New Trends in Fluorescence Spectroscopy: Applications to Chemical and Life Sciences. Springer Berlin Heidelberg. doi: 10.1007/978-3-642-56853-4
   Google Scholar
• Veselý, D., Veselá, D., & Jelínek, R. (1983). Comparative assessment of the aflatoxin B1, B2, G1, G2 and M1 embryotoxicity in the chick embryo. Toxicology Letters, 15(4), 297–300. doi: 10.1016/0378-4274(83)90147-9
   PubMed Web of Science ®Google Scholar
• Wang, R.-Q., Yin, Y.-J., Li, H., Wang, Y., Pu, J.-J., Wang, R., … Wang, R.-Y. (2013). Comparative study of the interactions between ovalbumin and three alkaloids by spectrofluorimetry. Molecular Biology Reports, 40(4), 3409–3418. doi: 10.1007/s11033-012-2418-x
   PubMed Web of Science ®Google Scholar
• Weijers, M., Sagis, L. M., Veerman, C., Sperber, B., & van der Linden, E. (2002). Rheology and structure of ovalbumin gels at low pH and low ionic strength. Food Hydrocolloids, 16(3), 269–276. (01)00097-2 doi: 10.1016/S0268-005X(01)00097-2
   Web of Science ®Google Scholar
• Wright, H. T., Qian, H. X., & Huber, R. (1990). Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin. Its relationship to the structure of cleaved alpha-1-proteinase inhibitor. Journal of Molecular Biology, 213(3), 513–528. doi: 10.1016/S0022-2836(05)80212-8
   PubMed Web of Science ®Google Scholar
• Xie, W., Wei, S., Liu, J., Ge, X., Zhou, L., Zhou, J., & Shen, J. (2014). Spectroscopic studies on the interaction of Ga3+-hypocrellin A with myoglobin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 121, 109–115. doi: 10.1016/j.saa.2013.10.085
   PubMed Web of Science ®Google Scholar
• Xu, X., Mao, X., Wang, Y., Li, D., Du, Z., Wu, W., … Li, J. (2018). Study on the interaction of graphene oxide-silver nanocomposites with bovine serum albumin and the formation of nanoparticle-protein corona. International Journal of Biological Macromolecules, 116, 492–501. doi: 10.1016/j.ijbiomac.2018.05.043
   PubMed Web of Science ®Google Scholar
• Yunus, A. W., Razzazi-Fazeli, E., Bohm, J., Yunus, A. W., Razzazi-Fazeli, E., & Bohm, J. (2011). Aflatoxin B1 in affecting broiler’s performance, immunity, and gastrointestinal tract: A review of history and contemporary issues. Toxins, 3(6), 566–590. doi: 10.3390/toxins3060566
   PubMed Web of Science ®Google Scholar