Glycation reduces the binding dynamics of aflatoxin B₁ to human serum albumin: a comprehensive spectroscopic and computational investigation

References

• Aamir Qureshi, M., & Javed, S. (2020). Structural dynamics studies on the binding of aflatoxin B1 to chicken egg albumin using spectroscopic techniques and molecular docking. Journal of Biomolecular Structure and Dynamics, 38(11), 3144–3155. https://doi.org/10.1080/07391102.2019.1652690
   PubMed Web of Science ®Google Scholar
• Ahmad, J., Raghav, A., Ahmad, J., Alam, K., & Khan, A. U. (2017). New insights into non-enzymatic glycation of human serum albumin biopolymer: A study to unveil its impaired structure and function. International Journal of Biological Macromolecules, 101, 84–99. https://doi.org/10.1016/j.ijbiomac.2017.03.086
   PubMed Web of Science ®Google Scholar
• Ali, M. S., & Al-Lohedan, H. A. (2019). Experimental and computational investigation on the molecular interactions of safranal with bovine serum albumin: Binding and anti-amyloidogenic efficacy of ligand. Journal of Molecular Liquids, 278, 385–393. https://doi.org/10.1016/j.molliq.2019.01.034
   Web of Science ®Google Scholar
• Ali, M. S., Muthukumaran, J., & Al-Lohedan, H. A. (2020). Molecular interactions of ceftazidime with bovine serum albumin: Spectroscopic, molecular docking, and DFT analyses. Journal of Molecular Liquids, 313, 113490. https://doi.org/10.1016/j.molliq.2020.113490
   Web of Science ®Google Scholar
• Amir, M., Qureshi, M. A., & Javed, S. (2021). Biomolecular interactions and binding dynamics of tyrosine kinase inhibitor erdafitinib, with human serum albumin. Journal of Biomolecular Structure and Dynamics, 39(11), 3934–3947. https://doi.org/10.1080/07391102.2020.1772880
   PubMed Web of Science ®Google Scholar
• Anguizola, J., Matsuda, R., Barnaby, O. S., Hoy, K. S., Wa, C., DeBolt, E., Koke, M., & Hage, D. S. (2013). Review: Glycation of human serum albumin. Clinica Chimica Acta; International Journal of Clinical Chemistry, 425, 64–76. https://doi.org/10.1016/j.cca.2013.07.013
   PubMed Web of Science ®Google Scholar
• Bagheri, F., & Fatemi, M. H. (2022). Investigation of the interaction between nilotinib and alpha-lactalbumin by spectroscopic methods and docking studies. Russian Journal of Bioorganic Chemistry, 48(4), 783–792. https://doi.org/10.1134/S1068162022040057
   Web of Science ®Google Scholar
• Bagheri, F., & Fatemi, M. H. (2021). Investigation of the interaction of sorafenib with alpha-lactalbumin: Spectroscopic and molecular modeling. Russian Journal of Bioorganic Chemistry, 47(4), 864–873. https://doi.org/10.1134/S1068162021040038
   Web of Science ®Google Scholar
• Barbosa, S., Taboada, P., & Mosquera, V. (2013). Fibrillation and polymorphism of human serum albumin. In Bio-nanoimaging: Protein misfolding and aggregation (pp. 345–362). Elsevier Inc. https://doi.org/10.1016/B978-0-12-394431-3.00032-8
   Google Scholar
• Bhat, S. A., Bhat, W. F., Arif, H., Afsar, M., Sohail, A., Khan, M. S., Rehman, M. T., Khan, R. A., & Bano, B. (2018). Glycation induced conformational transitions in cystatin proceed to form biotoxic aggregates: A multidimensional analysis. Biochimica et Biophysica Acta. Proteins and Proteomics, 1866(9), 989–1000. https://doi.org/10.1016/j.bbapap.2018.06.006
   PubMed Web of Science ®Google Scholar
• Bohlooli, M., Ghaffari-Moghaddam, M., Khajeh, M., & Sheibani, N. (2018). Determination of amadori product in glycated human serum albumin by spectroscopy methods. ChemistrySelect, 3(24), 7018–7022. https://doi.org/10.1002/slct.201800207
   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, 881(3), 383–390. https://doi.org/10.1016/0304-4165(86)90030-9
   PubMedGoogle Scholar
• Dockal, M., Carter, D. C., & Rüker, F. (1999). The three recombinant domains of human serum albumin. The Journal of Biological Chemistry, 274(41), 29303–29310. https://doi.org/10.1074/jbc.274.41.29303
   PubMed Web of Science ®Google Scholar
• Faisal, Z., Lemli, B., Szerencsés, D., Kunsági-Máté, S., Bálint, M., Hetényi, C., Kuzma, M., Mayer, M., & 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. https://doi.org/10.1007/s12550-018-0321-6
   PubMed Web of Science ®Google Scholar
• Furkan, M., Alam, M. T., Rizvi, A., Khan, K., Ali, A., Naeem., & A., Shamsuzzaman. (2017). Aloe emodin, an anthroquinone from Aloe vera acts as an anti aggregatory agent to the thermally aggregated hemoglobin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 179, 188–193. https://doi.org/10.1016/j.saa.2017.02.014
   PubMed Web of Science ®Google Scholar
• He, X. M., & Carter, D. C. (1992). Atomic structure and chemistry of human serum albumin. Nature, 358(6383), 209–215. https://doi.org/10.1038/358209a0
   PubMed Web of Science ®Google Scholar
• Hoseyni, P., Fatemi, M. H., Hadjmohammadi, M., & Majidi, S. M. (2022). Experimental and theoretical studies of the interactions of some synthetic food dyes with human serum albumin. Journal of the Iranian Chemical Society, 19(3), 885–892. https://doi.org/10.1007/s13738-021-02351-4
   Web of Science ®Google Scholar
• Hsieh, S. R., Reddy, P. M., Chang, C. J., Kumar, A., Wu, W. C., & Lin, H. Y. (2016). Exploring the behavior of bovine serum albumin in response to changes in the chemical composition of responsive polymers: Experimental and simulation studies. Polymer, 8, 238. https://doi.org/10.3390/POLYM8060238
   PubMed Web of Science ®Google Scholar
• Il’ichev, Y. V., Perry, J. L., & Simon, J. D. (2002). Interaction of ochratoxin A with human serum albumin. A common binding site of ochratoxin A and warfarin in subdomain IIA. Journal of Physical Chemistry B, 106, 460–465. https://doi.org/10.1021/jp012315m
   Web of Science ®Google Scholar
• Iqbal, S., Qais, F. A., Alam, M. M., & Naseem, I. (2018). Effect of glycation on human serum albumin–zinc interaction: A biophysical study. JBIC: Journal of Biological Inorganic Chemistry, 23(3), 447–458. https://doi.org/10.1007/s00775-018-1554-8
   PubMed Web of Science ®Google Scholar
• Jahanban-Esfahlan, A., Panahi-Azar, V., & Sajedi, S. (2016). Interaction of glutathione with bovine serum albumin: Spectroscopy and molecular docking. Food Chemistry, 202, 426–431. https://doi.org/10.1016/j.foodchem.2016.02.026
   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. https://doi.org/10.1016/j.jpba.2005.11.037
   PubMed Web of Science ®Google Scholar
• Khan, M. W. A., Rasheed, Z., Khan, W. A., & Ali, R. (2007). Biochemical, biophysical, and thermodynamic analysis of in vitro glycated human serum albumin. Biochemistry, 72, 146–152. https://doi.org/10.1134/S0006297907020034
   PubMed Web of Science ®Google Scholar
• Lakowicz, J. R. (2006). Principles of fluorescence spectroscopy (3rd ed.). In Principles of Fluorescence Spectroscopy. Springer. https://doi.org/10.1007/978-0-387-46312-4
   Google Scholar
• Lapolla, A., Fedele, D., Reitano, R., Bonfante, L., Guizzo, M., Seraglia, R., Tubaro, M., & Traldi, P. (2005). Mass spectrometric study of in vivo production of advanced glycation end-products/peptides. Journal of Mass Spectrometry, 40(7), 969–972. https://doi.org/10.1002/jms.842
   PubMed Web of Science ®Google Scholar
• Lee, P., & Wu, X. (2015). Review: Modifications of human serum albumin and their binding effect. Current Pharmaceutical Design, 21(14), 1862–1865. https://doi.org/10.2174/1381612821666150302115025
   PubMed Web of Science ®Google Scholar
• Levitt, D. G., & Levitt, M. D. (2016). Human serum albumin homeostasis: A new look at the roles of synthesis, catabolism, renal and gastrointestinal excretion, and the clinical value of serum albumin measurements. International Journal of General Medicine, 9, 229–255. https://doi.org/10.2147/IJGM.S102819
   PubMed Web of Science ®Google Scholar
• Liang, G.-W., Chen, Y.-C., Wang, Y., Wang, H.-M., Pan, X.-Y., Chen, P.-H., & Niu, Q.-X. (2018). Interaction between saikosaponin D, paeoniflorin, and human serum albumin. Molecules, 23(2), 249. https://doi.org/10.3390/molecules23020249
   PubMed Web of Science ®Google Scholar
• Lou, Y. Y., Zhou, K. L., Pan, D. Q., Le Shen, J., & Shi, J. H. (2017). Spectroscopic and molecular docking approaches for investigating conformation and binding characteristics of clonazepam with bovine serum albumin (BSA). Journal of Photochemistry and Photobiology B: Biology, 167, 158–167. https://doi.org/10.1016/j.jphotobiol.2016.12.029
   PubMed Web of Science ®Google Scholar
• Lu, H., Liu, F., Zhu, Q., Zhang, M., Li, T., Chen, J., Huang, Y., Wang, X., & Sheng, J. (2017). Aflatoxin B1 can be complexed with oxidised tea polyphenols and the absorption of the complexed aflatoxin B1 is inhibited in rats. Journal of the Science of Food and Agriculture, 97(6), 1910–1915. https://doi.org/10.1002/jsfa.7994
   PubMed Web of Science ®Google Scholar
• Marchese, S., Polo, A., Ariano, A., Velotto, S., & Costantini, S. (2018). Aflatoxin B1 and M1: Biological properties and their involvement in cancer development. Toxins Reviews, 10(6), 1–19. https://doi.org/10.3390/toxins10060214
   Google Scholar
• Milk, P., & Itano, E. N. (2016). Exposure assessment of infants to aflatoxin M 1 through consumption of breast milk and infant. Toxins (Basel), 1, 1–11. https://doi.org/10.3390/toxins8090246
   Google Scholar
• Musa, K. A., Ning, T., Mohamad, S. B., & Tayyab, S. (2020). Intermolecular recognition between pyrimethamine, an antimalarial drug and human serum albumin: Spectroscopic and docking study. Journal of Molecular Liquids, 311, 113270. https://doi.org/10.1016/j.molliq.2020.113270
   Web of Science ®Google Scholar
• Mykkänen, H., Zhu, H., Salminen, E., Juvonen, R. O., Ling, W., Ma, J., Polychronaki, N., Kemiläinen, H., Mykkänen, O., Salminen, S., & El-Nezami, H. (2005). Fecal and urinary excretion of aflatoxin B1 metabolites (AFQ1, AFM1 and AFB-N7-guanine) in young Chinese males. International Journal of Cancer, 115(6), 879–884. https://doi.org/10.1002/ijc.20951
   PubMed Web of Science ®Google Scholar
• Ndzibongwana, S., Ngobese, S., Sayed, A., Shongwe, C., White-Phillips, S., & Joubert, J. (2019). Structural analysis, molecular modelling and preliminary competition binding studies of AM-DAN as a NMDA receptor PCP-site fluorescent ligand. Molecules, 24(22), 4092. https://doi.org/10.3390/molecules24224092
   PubMed Web of Science ®Google Scholar
• Neelofar, K., Arif, Z., Ahmad, J., & Alam, K. (2019). Inhibitory effect of silibinin on amadori-albumin in diabetes mellitus: A multi-spectroscopic and biochemical approach. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 209, 217–222. https://doi.org/10.1016/j.saa.2018.10.044
   PubMed Web of Science ®Google Scholar
• Nusrat, S., Siddiqi, M. K., Zaman, M., Zaidi, N., Rehan Ajmal, M., Alam, P., Qadeer, A., Saber Abdelhameed, A., & Hasan Khan, R. (2016). A comprehensive spectroscopic and computational investigation to probe the interaction of antineoplastic drug nordihydroguaiaretic acid with serum albumins. 11(7), e0158833. https://doi.org/10.1371/journal.pone.0158833
   Google Scholar
• Paul, S., Ghanti, R., Sardar, P. S., & Majhi, A. (2019). Synthesis of a novel coumarin derivative and its binding interaction with serum albumins. Chemistry of Heterocyclic Compounds, 55(7), 607–611. https://doi.org/10.1007/s10593-019-02505-6
   Web of Science ®Google Scholar
• Pestka, J. J., & Chu, F. S. (1984). Aflatoxin B1dihydrodiol antibody: Production and specificity. Applied and Environmental Microbiology, 47(3), 472–477. https://doi.org/10.1128/aem.47.3.472-477.1984
   PubMed Web of Science ®Google Scholar
• Poór, M., Kunsági-Máté, S., Bálint, M., Hetényi, C., Gerner, Z., & Lemli, B. (2017). Interaction of mycotoxin zearalenone with human serum albumin. Journal of Photochemistry and Photobiology B: Biology, 170, 16–24. https://doi.org/10.1016/j.jphotobiol.2017.03.016
   PubMed Web of Science ®Google Scholar
• Qureshi, M. A., & Javed, S. (2022). Investigating binding dynamics of trans resveratrol to HSA for an efficient displacement of aflatoxin B1 using spectroscopy and molecular simulation. Scientific Reports 2022, 12, 1–17. https://doi.org/10.1038/s41598-022-06375-5
   PubMed Web of Science ®Google Scholar
• Qureshi, M. A., & Javed, S. (2021). Aflatoxin B 1 induced structural and conformational changes in bovine serum albumin: A multispectroscopic and circular dichroism-based study. ACS Omega, 6(28), 18054–18064. https://doi.org/10.1021/acsomega.1c01799
   PubMed 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. https://doi.org/10.1021/bi00514a017
   PubMed Web of Science ®Google Scholar
• Rostamnezhad, F., & Hossein Fatemi, M. (2022). Comprehensive investigation of binding of some polycyclic aromatic hydrocarbons with bovine serum albumin: Spectroscopic and molecular docking studies. Bioorganic Chemistry, 120, 105656. https://doi.org/10.1016/j.bioorg.2022.105656
   PubMed Web of Science ®Google Scholar
• Salim, M. M., El Sharkasy, M. E., Belal, F., & Walash, M. (2021). Multi-spectroscopic and molecular docking studies for binding interaction between fluvoxamine and human serum albumin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 252, 119495. https://doi.org/10.1016/j.saa.2021.119495
   PubMed Web of Science ®Google Scholar
• Schmitt, A., Schmitt, J., Münch, G., & Gasic-Milencovic, J. (2005). Characterization of advanced glycation end products for biochemical studies: Side chain modifications and fluorescence characteristics. Analytical Biochemistry, 338(2), 201–215. https://doi.org/10.1016/j.ab.2004.12.003
   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 Luminescense, 151, 206–218. https://doi.org/10.1016/j.jlumin.2014.02.009
   Web of Science ®Google Scholar
• Selva Sharma, A., & Ilanchelian, M. (2015). Comprehensive multispectroscopic analysis on the interaction and corona formation of human serum albumin with gold/silver alloy nanoparticles. The Journal of Physical Chemistry B, 119(30), 9461–9476. https://doi.org/10.1021/acs.jpcb.5b00436
   PubMed Web of Science ®Google Scholar
• Shen, Y., Zhu, C., Wang, Y., Xu, J., Xue, R., Ji, F., Wu, Y., Wu, Z., Zhang, W., Zheng, Z., & Ye, Y. (2020). Evaluation the binding of chelerythrine, a potentially harmful toxin, with bovine serum albumin. Food and Chemical Toxicology, 135, 110933. https://doi.org/10.1016/j.fct.2019.110933
   PubMed Web of Science ®Google Scholar
• Siddiqui, M. F., & Bano, B. (2018). Exposure of carbendazim induces structural and functional alteration in garlic phytocystatin: An in vitro multi-spectroscopic approach. Pesticide Biochemistry and Physiology, 145, 66–75. https://doi.org/10.1016/j.pestbp.2018.01.008
   PubMed Web of Science ®Google Scholar
• Siddiqui, S., Ameen, F., Jahan, I., Nayeem, S. M., & Tabish, M. (2019). A comprehensive spectroscopic and computational investigation on the binding of the anti-asthmatic drug triamcinolone with serum albumin. New Journal of Chemistry, 43(10), 4137–4151. https://doi.org/10.1039/C8NJ05486J
   Web of Science ®Google Scholar
• Singh, I., Luxami, V., & Paul, K. (2020). Spectroscopy and molecular docking approach for investigation on the binding of nocodazole to human serum albumin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 235, 118289. https://doi.org/10.1016/j.saa.2020.118289
   PubMed Web of Science ®Google Scholar
• Singha Roy, A., Pandey, N. K., & Dasgupta, S. (2013). Preferential binding of fisetin to the native state of bovine serum albumin: Spectroscopic and docking studies. Molecular Biology Reports, 40(4), 3239–3253. https://doi.org/10.1007/s11033-012-2399-9
   PubMed Web of Science ®Google Scholar
• Singla, R., Abidi, S. M. S., Dar, A. I., & Acharya, A. (2019). Inhibition of glycation-induced aggregation of human serum albumin by organic-inorganic hybrid nanocomposites of iron oxide-functionalized nanocellulose. ACS Omega, 4(12), 14805–14819. https://doi.org/10.1021/acsomega.9b01392
   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.
   PubMed Web of Science ®Google Scholar
• Tabassum, S., Al-Asbahy, W. M., Afzal, M., & Arjmand, F. (2012). Synthesis, characterization and interaction studies of copper based drug with human serum albumin (HSA): Spectroscopic and molecular docking investigations. Journal of Photochemistry and Photobiology B: Biology, 114, 132–139. https://doi.org/10.1016/j.jphotobiol.2012.05.021
   PubMed Web of Science ®Google Scholar
• Tan, H., Chen, L., Ma, L., Liu, S., Zhou, H., Zhang, Y., Guo, T., Liu, W., Dai, H., & Yu, Y. (2019). Fluorescence spectroscopic investigation of competitive interactions between quercetin and aflatoxin B1 for binding to human serum albumin. Toxins (Basel), 11(4), 214. https://doi.org/10.3390/toxins11040214
   PubMed Web of Science ®Google Scholar
• Tao, P., Li, Z., Woolfork, A. G., & Hage, D. S. (2019). Characterization of tolazamide binding with glycated and normal human serum albumin by using high-performance affinity chromatography. Journal of Pharmaceutical and Biomedical Analysis, 166, 273–280. https://doi.org/10.1016/j.jpba.2019.01.025
   PubMed Web of Science ®Google Scholar
• Taverna, M., Marie, A. L., Mira, J. P., & Guidet, B. (2013). Specific antioxidant properties of human serum albumin. Annals of Intensive Care, 3(1), 4. https://doi.org/10.1186/2110-5820-3-4
   PubMed Web of Science ®Google Scholar
• Thornalley, P. J., Langborg, A., & Minhas, H. S. (1999). Formation of glyoxal, methylglyoxal and 8-deoxyglucosone in the glycation of proteins by glucose. Biochemical Journal, 344(1), 109–116. https://doi.org/10.1042/0264-6021:3440109
   PubMedGoogle Scholar
• Trynda-Lemiesz, L., & Wiglusz, K. (2011). Effects of glycation on meloxicam binding to human serum albumin. Journal of Molecular Structure, 995(1–3), 35–40. https://doi.org/10.1016/j.molstruc.2011.03.037
   Web of Science ®Google Scholar
• Wangia, R. N., Tang, L., & Wang, J.-S. (2019). Occupational exposure to aflatoxins and health outcomes: A review. Journal of Environmental Health Science. Part C, 37(4), 215–234. https://doi.org/10.1080/10590501.2019.1664836
   PubMedGoogle Scholar
• Wu, D., Wang, J., Liu, D., Zhang, Y., & Hu, X. (2019). Computational and spectroscopic analysis of interaction between food colorant citrus red 2 and human serum albumin. Scientific Reports, 9, 1–8. https://doi.org/10.1038/s41598-018-38240-9
   PubMed Web of Science ®Google Scholar
• Xu, L., Hu, Y. X., Li, Y. C., Liu, Y. F., Zhang, L., Ai, H. X., & Liu, H. S. (2017). Study on the interaction of paeoniflorin with human serum albumin (HSA) by spectroscopic and molecular docking techniques. Chemistry Central Journal, 11(1), 116. https://doi.org/10.1186/s13065-017-0348-3
   PubMedGoogle Scholar
• Yadav, P., Sharma, B., Sharma, C., Singh, P., & Awasthi, S. K. (2020). Interaction between the antimalarial drug dispiro-tetraoxanes and human serum albumin: A combined study with spectroscopic methods and computational studies. ACS Omega, 5(12), 6472–6480. https://doi.org/10.1021/acsomega.9b04095
   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 (Basel), 3(6), 566–590. https://doi.org/10.3390/toxins3060566
   PubMed Web of Science ®Google Scholar
• Zhang, Z., Yang, M., Yi, J., Zhu, Q., Huang, C., Chen, Y., Li, J., Yang, B., & Zhao, X. (2019). Comprehensive insights into the interactions of two emerging bromophenolic DBPs with human serum albumin by multispectroscopy and molecular docking. ACS Omega, 4(1), 563–572. https://doi.org/10.1021/acsomega.8b03116
   Web of Science ®Google Scholar