Interactions of tetracyclines with milk allergenic protein (casein): a molecular and biological approach

References

• Abdelhameed, A. S., Alanazi, A. M., Bakheit, A. H., Darwish, H. W., Ghabbour, H. A., & Darwish, I. A. (2017). Fluorescence spectroscopic and molecular docking studies of the binding interaction between the new anaplastic lymphoma kinase inhibitor crizotinib and bovine serum albumin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 171, 174–182. doi:10.1016/j.saa.2016.08.005
   PubMed Web of Science ®Google Scholar
• Albani, J. R. (2007). Principles and applications of fluorescence spectroscopy. United Kingdom: Blackwell Publishing. doi:10.1002/9780470692059
   Google Scholar
• Allahdad, Z., Varidi, M., Zadmard, R., & Saboury, A. A. (2018). Spectroscopic and docking studies on the interaction between caseins and β-carotene. Food Chemistry, 255, 187–196. doi:10.1016/j.foodchem.2018.01.143
   PubMed Web of Science ®Google Scholar
• Antonov, Y. A., Moldenaers, P., & Cardinaels, R. (2017). Complexation of lysozyme with sodium caseinate and micellar casein in aqueous buffered solutions. Food Hydrocolloids, 62, 102–118. doi:10.1016/j.foodhyd.2016.07.012
   Web of Science ®Google Scholar
• Arroyo-Maya, I. J., Campos-Terán, J., Hernández-Arana, A., & McClements, D. J. (2016). Characterization of flavonoid-protein interactions using fluorescence spectroscopy: Binding of pelargonidin to dairy proteins. Food Chemistry, 213, 431–439. doi:10.1016/j.foodchem.2016.06.105
   PubMed Web of Science ®Google Scholar
• Audic, J.-L., & Chaufer, B. (2005). Influence of plasticizers and crosslinking on the properties of biodegradable films made from sodium caseinate. European Polymer Journal, 41(8), 1934–1942. doi:10.1016/j.eurpolymj.2005.02.023
   Web of Science ®Google Scholar
• Barreca, D., Laganà, G., Toscano, G., Calandra, P., Kiselev, M. A., Lombardo, D., & Bellocco, E. (2017). The interaction and binding of flavonoids to human serum albumin modify its conformation, stability and resistance against aggregation and oxidative injuries. Biochimica et Biophysica Acta (BBA)—General Subjects, 1861(1), 3531–3539. doi:10.1016/j.bbagen.2016.03.014
   PubMed Web of Science ®Google Scholar
• Bhattacharya, M. & Mukhopadhyay, S. (2012). Structural and dynamical insights into the molten-globule form of ovalbumin. The Journal of Physical Chemistry B, 116, 520–531. doi:10.1021/jp208416d
   PubMed Web of Science ®Google Scholar
• Bi, H., Tang, L., Gao, X., Jia, J., & Lv, H. (2016). Spectroscopic analysis on the binding interaction between tetracycline hydrochloride and bovine proteins β-casein, α-lactalbumin. Journal of Luminescence, 178, 72–83. doi:10.1016/j.jlumin.2016.05.048
   Web of Science ®Google Scholar
• Bogahawaththa, D., Ashraf, R., Chandrapala, J., Donkor, O., & Vasiljevic, T. (2018). In vitro immunogenicity of various native and thermally processed bovine milk proteins and their mixtures. Journal of Dairy Science, 101(10), 8726–8736. doi:10.3168/jds.2018-14488
   PubMed Web of Science ®Google Scholar
• Bogahawaththa, D., Chandrapala, J., & Vasiljevic, T. (2017). Modulation of milk immunogenicity by thermal processing. International Dairy Journal, 69, 23–32. doi:10.1016/j.idairyj.2017.01.010
   Web of Science ®Google Scholar
• Bohin, M. C., Vincken, J.-P., Westphal, A. H., Tripp, A. M., Dekker, P., van der Hijden, H. T. W. M., & Gruppen, H. (2014). Interaction of flavan-3-ol derivatives and different caseins is determined by more than proline content and number of proline repeats. Food Chemistry, 158, 408–416. doi:10.1016/j.foodchem.2014.02.145
   PubMed Web of Science ®Google Scholar
• Bojko, B., Sułkowska, A., Maciążek-Jurczyk, M., Równicka, J., & Sułkowski, W. W. (2009). Investigations of acetaminophen binding to bovine serum albumin in the presence of fatty acid: Fluorescence and 1H NMR studies. Journal of Molecular Structure, 924–926, 332–337. doi:10.1016/j.molstruc.2008.12.015
   Web of Science ®Google Scholar
• Brandão, E., Santos Silva, M., García-Estévez, I., Mateus, N., de Freitas, V., & Soares, S. (2017). Molecular study of mucin-procyanidin interaction by fluorescence quenching and saturation transfer difference (STD)-NMR. Food Chemistry, 228, 427–434. doi:10.1016/j.foodchem.2017.02.027
   PubMed Web of Science ®Google Scholar
• Celotti, M., & Fazakerley, G. V. (1977). Conformation of various tetracycline species determined with the aid of a nuclear magnetic resonance relaxation probe. Journal of the Chemical Society, Perkin Transactions, 2(10), 1319. doi:10.1039/p29770001319
   Google Scholar
• Chen, F., Yin, J., Wang, Y., Yang, M., Meng, Q., Zeng, B., … Liu, J. (2015). Interaction of L-arginine with κ-casein and its effect on amyloid fibril formation by the protein: Multi-spectroscopic approaches. Journal of Photochemistry and Photobiology B: Biology, 143, 130–138. doi:10.1016/j.jphotobiol.2015.01.006
   PubMed Web of Science ®Google Scholar
• Damadoran, S., Parkin, K. L., & Fennema, O. R. (2010). Quimica de Alimentos de Fennema (4a). Porto Alegre, RS: Artmed.
   Google Scholar
• Dantas, M. D., de, A., Tenório, H., de, 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
• Das, S., Pahari, S., Sarmah, S., Rohman, M. A., Paul, D., Jana, M., & Singha Roy, A. (2019). Lysozyme–luteolin binding: Molecular insights into the complexation process and the inhibitory effects of luteolin towards protein modification. Physical Chemistry Chemical Physics, 21(23), 12649–12666. doi:10.1039/C9CP01128E
   PubMed Web of Science ®Google Scholar
• Dezhampanah, H., Esmaili, M., & Jampour, S. (2019). Spectroscopic and molecular docking studies on interaction of two Schiff base complexes with bovine serum albumin. Journal of Biomolecular Structure and Dynamics, 1–9. doi:10.1080/07391102.2019.1639548
   PubMedGoogle Scholar
• Dezhampanah, H., Esmaili, M., & Khorshidi, A. (2017a). A combination of spectroscopic and molecular docking techniques to study interaction of bis(indolyl)methane with bovine milk α-casein. International Journal of Food Properties, 20 (11), 2686–2698. doi:10.1080/10942912.2016.1247857
   Web of Science ®Google Scholar
• Dezhampanah, H., Esmaili, M., & Khorshidi, A. (2017b). Milk β-casein as a vehicle for delivery of bis(indolyl)methane: Spectroscopy and molecular docking studies. Journal of Molecular Structure, 1136, 50–58. doi:10.1016/j.molstruc.2017.01.065
   Web of Science ®Google Scholar
• Ettelaie, R., Khandelwal, N., & Wilkinson, R. (2014). Interactions between casein layers adsorbed on hydrophobic surfaces from self consistent field theory: κ-casein versus para-κ-casein. Food Hydrocolloids, 34, 236–246. doi:10.1016/j.foodhyd.2012.09.006
   Web of Science ®Google Scholar
• Ferraro, M. J. & National Committee for Clinical Laboratory Standards. (2003). Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically: Supplemental tables: approved standard. Wayne, PA: National Committee for Clinical Laboratory Standard.
   Google Scholar
• Figueiredo, I. M., & Marsaioli, A. J. (2007). Mapeamento das interações proteína-ligante através de técnicas de RMN de 1H utilizando detecção do ligante. Química Nova, 30(7), 1597–1605. doi:10.1590/S0100-40422007000700019
   Google Scholar
• Gonzalez, W. G., & Miksovska, J. (2014). Application of ANS fluorescent probes to identify hydrophobic sites on the surface of DREAM. Biochimica et Biophysica Acta (BBA)—Proteins and Proteomics, 1844(9), 1472–1480. doi:10.1016/j.bbapap.2014.05.004
   PubMed Web of Science ®Google Scholar
• Guerra, W., Silva-Caldeira, P. P., Terenzi, H., & Pereira-Maia, E. C. (2016). Impact of metal coordination on the antibiotic and non-antibiotic activities of tetracycline-based drugs. Coordination Chemistry Reviews, 327–328, 188–199. doi:10.1016/j.ccr.2016.04.009
   Web of Science ®Google Scholar
• He, W., Xu, H., Lu, Y., Zhang, T., Li, S., Lin, X., … Wu, X. (2019). Function, digestibility and allergenicity assessment of ovalbumin-EGCG conjugates. Journal of Functional Foods, 61, 103490, 1–10. doi:10.1016/j.jff.2019.103490
   Web of Science ®Google Scholar
• He, Z., Xu, M., Zeng, M., Qin, F., & Chen, J. (2016). Interactions of milk α- and β-casein with malvidin-3-O-glucoside and their effects on the stability of grape skin anthocyanin extracts. Food Chemistry, 199, 314–322. doi:10.1016/j.foodchem.2015.12.035
   PubMed Web of Science ®Google Scholar
• Hsu, L.-C., Liu, Y.-T., Syu, C.-H., Huang, M.-H., Tzou, Y.-M., & Teah, H. Y. (2018). Adsorption of tetracycline on Fe (hydr)oxides: Effects of pH and metal cation (Cu2+, Zn2+ and Al3+) addition in various molar ratios. Royal Society Open Science, 5 (3), 171941–171912. doi:10.6084/m9.figshare.c.4028170.
   PubMed Web of Science ®Google Scholar
• Kalyankar, S. D., Khedkar, C. D., Patil, A. M., & Deosarkar, S. S. (2016). Milk: Sources and composition. In Encyclopedia of food and health (pp. 741–747). Amsterdam, Netherlands: Elsevier. doi:10.1016/B978-0-12-384947-2.00463-3
   Google Scholar
• Kang, J., Liu, H., Zheng, Y.-M., Qu, J., & Chen, J. P. (2011). Application of nuclear magnetic resonance spectroscopy, Fourier transform infrared spectroscopy, UV–Visible spectroscopy and kinetic modeling for elucidation of adsorption chemistry in uptake of tetracycline by zeolite beta. Journal of Colloid and Interface Science, 354(1), 261–267.
   PubMed Web of Science ®Google Scholar
• Kang, D., Ryu, S. R., Park, Y., Czarnik-Matusewicz, B., & Jung, Y. M. (2014). pH-induced structural changes of ovalbumin studied by 2D correlation IR spectroscopy. Journal of Molecular Structure, 1069, 299–304. doi:10.1016/j.molstruc.2014.02.061
   Web of Science ®Google Scholar
• Khan, A. B., Khan, J. M., Ali, M. S. & Khan, R. H. (2012). Interaction of amphiphilic drugs with human and bovine serum albumins. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 97, 119–124. doi:10.1016/j.saa.2012.05.060
   PubMed Web of Science ®Google Scholar
• Kuang, Y., Jia, H., Miyanaga, K., & Tanji, Y. (2009). Effect of milk on antibacterial activity of tetracycline against Escherichia coli and Staphylococcus aureus isolated from bovine mastitis. Applied Microbiology and Biotechnology, 84(1), 135–142. doi:10.1007/s00253-009-2008-6
   PubMed Web of Science ®Google Scholar
• Lage, T. C. A., Maciel, T. M. S., Mota, Y. C. C., Sisto, F., Sabino, J. R., Santos, J. C. C., … Modolo, L. V. (2018). In vitro inhibition of Helicobacter pylori and interaction studies of lichen natural products with jack bean urease. New Journal of Chemistry, 42(7), 5356–5366. doi:10.1039/C8NJ00072G
   Web of Science ®Google Scholar
• Lakowicz, J. R. (2006). Principles of fluorescence spectroscopy (3rd ed.). Baltimore: Springer.
   Google Scholar
• Li, D., Zhang, T., & Ji, B. (2014). Influences of pH, urea and metal ions on the interaction of sinomenine with Lysozyme by steady state fluorescence spectroscopy. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 130, 440–446. doi:10.1016/j.saa.2014.04.054
   PubMed Web of Science ®Google Scholar
• Li, T., Cheng, Z., Cao, L., & Jiang, X. (2016). Comparison of interactions between three food colorants and BSA. Food Chemistry, 194, 740–748. doi:10.1016/j.foodchem.2015.08.067.
   PubMed Web of Science ®Google Scholar
• Liang, J., Cheng, Y., & Han, H. (2008). Study on the interaction between bovine serum albumin and CdTe quantum dots with spectroscopic techniques. Journal of Molecular Structure, 892(1–3), 116–120. doi:10.1016/j.molstruc.2008.05.005
   Web of Science ®Google Scholar
• Lou, Y.-Y., Zhou, K.-L., Pan, D.-Q., Shen, J.-L., & 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. doi:10.1016/j.jphotobiol.2016.12.029
   PubMed Web of Science ®Google Scholar
• Massella, E., Piva, S., Giacometti, F., Liuzzo, G., Zambrini, A. V., & Serraino, A. (2017). Evaluation of bovine beta casein polymorphism in two dairy farms located in northern Italy. Italian Journal of Food Safety, 6(3), 6904. doi:10.4081/ijfs.2017.6904
   PubMed Web of Science ®Google Scholar
• Mediwaththe, A., Bogahawaththa, D., Grewal, M. K., Chandrapala, J., & Vasiljevic, T. (2018). Structural changes of native milk proteins subjected to controlled shearing and heating. Food Research International, 114, 151–158. doi:10.1016/j.foodres.2018.08.001
   PubMed Web of Science ®Google Scholar
• Mehranfar, F., Bordbar, A.-K., Fani, N., & Keyhanfar, M. (2013). Binding analysis for interaction of diacetylcurcumin with β-casein nanoparticles by using fluorescence spectroscopy and molecular docking calculations. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 115, 629–635. doi:10.1016/j.saa.2013.06.062
   PubMed Web of Science ®Google Scholar
• Miciński, J., Kowalski, I. M., Zwierzchowski, G., Szarek, J., Pierożyński, B., & Zabłocka, E. (2013). Characteristics of cow’s milk proteins including allergenic properties and methods for its reduction. Polish Annals of Medicine, 20(1), 69–76. doi:10.1016/j.poamed.2013.07.006
   Google Scholar
• Moeiniafshari, A.-A., Zarrabi, A., & Bordbar, A.-K. (2015). Exploring the interaction of naringenin with bovine beta-casein nanoparticles using spectroscopy. Food Hydrocolloids, 51, 1–6. doi:10.1016/j.foodhyd.2015.04.036
   Web of Science ®Google Scholar
• Mondal, M., Lakshmi, P., Krishna, R., & Sakthivel, N. (2017). Molecular interaction between human serum albumin (HSA) and phloroglucinol derivative that shows selective anti-proliferative potential. Journal of Luminescence, 192, 990–998. doi:10.1016/j.jlumin.2017.08.007
   Web of Science ®Google Scholar
• Mushtaq, S., Shah, A. M., Shah, A., Lone, S. A., Hussain, A., Hassan, Q. P., & Ali, M. N. (2018). Bovine mastitis: An appraisal of its alternative herbal cure. Microbial Pathogenesis, 114, 357–361. doi:10.1016/j.micpath.2017.12.024
   PubMed Web of Science ®Google Scholar
• Nebot, C., Guarddon, M., Seco, F., Iglesias, A., Miranda, J. M., Franco, C. M., & Cepeda, A. (2014). Monitoring the presence of residues of tetracyclines in baby food samples by HPLC-MS/MS. Food Control, 46, 495–501. doi:10.1016/j.foodcont.2014.05.042
   Web of Science ®Google Scholar
• Pal, S., Woodford, K., Kukuljan, S., & Ho, S. (2015). Milk Intolerance, Beta-Casein and Lactose. Nutrients, 7(9), 7285–7297. doi:10.3390/nu7095339
   PubMed Web of Science ®Google Scholar
• Poureshghi, F., Ghandforoushan, P., Safarnejad, A., & Soltani, S. (2017). Interaction of an antiepileptic drug, lamotrigine with human serum albumin (HSA): Application of spectroscopic techniques and molecular modeling methods. Journal of Photochemistry and Photobiology B: Biology, 166, 187–192. doi:10.1016/j.jphotobiol.2016.09.046
   PubMed Web of Science ®Google Scholar
• Pulicharla, R., Hegde, K., Brar, S. K., & Surampalli, R. Y. (2017). Tetracyclines metal complexation: Significance and fate of mutual existence in the environment. Environmental Pollution, 221, 1–14. doi:10.1016/j.envpol.2016.12.017
   PubMed Web of Science ®Google Scholar
• Rabbani, G., Baig, M. H., Jan, A. T., Ju Lee, E., Khan, M. V., Zaman, M., … Choi, I. (2017). Binding of erucic acid with human serum albumin using a spectroscopic and molecular docking study. International Journal of Biological Macromolecules, 105, 1572–1580. doi:10.1016/j.ijbiomac.2017.04.051
   PubMed Web of Science ®Google Scholar
• Ranjbar, S., Shokoohinia, Y., Ghobadi, S., Bijari, N., Gholamzadeh, S., Moradi, N., … Khodarahmi, R. (2013). Studies of the interaction between isoimperatorin and human serum albumin by multispectroscopic method: Identification of possible binding site of the compound using esterase activity of the protein. The Scientific World Journal, 2013, 1–13. doi:10.1155/2013/305081
   Google Scholar
• Ridout, M. J., Paananen, A., Mamode, A., Linder, M. B., & Wilde, P. J. (2015). Interaction of transglutaminase with adsorbed and spread films of β-casein and к-casein. Colloids and Surfaces B: Biointerfaces, 128, 254–260. doi:10.1016/j.colsurfb.2015.01.045
   PubMed Web of Science ®Google Scholar
• Santana, C. C., Silva-Júnior, E. F., Santos, J. C. N., Rodrigues, É. E. D S., da Silva, I. M., Araújo-Júnior, J. X., … Grillo, L. A. M. (2019). Evaluation of guanylhydrazone derivatives as inhibitors of Candida rugosa digestive lipase: Biological, biophysical, theoretical studies and biotechnological application. Bioorganic Chemistry, 87, 169–180. doi:10.1016/j.bioorg.2019.03.030
   PubMed Web of Science ®Google Scholar
• Santos, J. C. N., da Silva, I. M., Braga, T. C., de Fátima, Â., Figueiredo, I. M., & Santos, J. C. C. (2018). Thimerosal changes protein conformation and increase the rate of fibrillation in physiological conditions: Spectroscopic studies using bovine serum albumin (BSA). International Journal of Biological Macromolecules, 113, 1032–1040. doi:10.1016/j.ijbiomac.2018.02.116
   PubMed Web of Science ®Google Scholar
• Shahabadi, N., Hakimi, M., Morovati, T., Hadidi, S., & Moeini, K. (2017). Spectroscopic investigation into the interaction of a diazacyclam-based macrocyclic copper(ii) complex with bovine serum albumin: Metal complex protein interaction. Luminescence, 32(1), 43–50. doi:10.1002/bio.3146
   PubMed Web of Science ®Google Scholar
• Shi, J.-H., Lou, Y.-Y., Zhou, K.-L., & Pan, D.-Q. (2018). Elucidation of intermolecular interaction of bovine serum albumin with Fenhexamid: A biophysical prospect. Journal of Photochemistry and Photobiology B: Biology, 180, 125–133. doi:10.1016/j.jphotobiol.2018.01.025
   PubMed Web of Science ®Google Scholar
• Siddiqi, M., Nusrat, S., Alam, P., Malik, S., Chaturvedi, S. K., Ajmal, M. R., … Khan, R. H. (2018). Investigating the site selective binding of busulfan to human serum albumin: Biophysical and molecular docking approaches. International Journal of Biological Macromolecules, 107, 1414–1421. doi:10.1016/j.ijbiomac.2017.10.006
   PubMed Web of Science ®Google Scholar
• Sun, H., & Pan, Y.-C. E. (1999). Using native gel in two-dimensional PAGE for the detection of protein interactions in protein extract. Journal of Biochemical and Biophysical Methods, 39(3), 143–151. doi:10.1016/S0165-022X(99)00009-3
   PubMedGoogle Scholar
• Verhoeckx, K. C. M., Vissers, Y. M., Baumert, J. L., Faludi, R., Feys, M., Flanagan, S., … Kimber, I. (2015). Food processing and allergenicity. Food and Chemical Toxicology, 80, 223–240. doi:10.1016/j.fct.2015.03.005
   PubMed Web of Science ®Google Scholar
• Vincent, D., Elkins, A., Condina, M. R., Ezernieks, V., & Rochfort, S. (2016). Quantitation and Identification of Intact Major Milk Proteins for High-Throughput LC-ESI-Q-TOF MS Analyses. Plos One, 11(10), e0163471. doi:10.1371/journal.pone.0163471
   PubMed Web of Science ®Google Scholar
• Wang, J., Ma, L., Zhang, Y., & Jiang, T. (2017). Investigation of the interaction of deltamethrin (DM) with human serum albumin by multi-spectroscopic method. Journal of Molecular Structure, 1129, 160–168. doi:10.1016/j.molstruc.2016.09.061
   Web of Science ®Google Scholar
• Wang, R., Li, Z., Yang, L., Ren, T., Zhang, L., & Wang, R. (2015). Studies on the interaction between neutral red and bovine hemoglobin by fluorescence spectroscopy and molecular modeling. Journal of Molecular Liquids, 211, 584–590. doi:10.1016/j.molliq.2015.07.066
   Web of Science ®Google Scholar
• Wang, Y., Jiang, X., Zhou, L., Yang, L., Xia, G., Chen, Z., & Duan, M. (2013). Synthesis and binding with BSA of a new gemini surfactant. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 436, 1159–1169. doi:10.1016/j.colsurfa.2013.08.045
   Web of Science ®Google Scholar
• Wei, J., Xu, D., Yang, J., Zhang, X., Mu, T., & Wang, Q. (2018). Analysis of the interaction mechanism of Anthocyanins (Aronia melanocarpa Elliot) with β-casein. Food Hydrocolloids, 84, 276–281. doi:10.1016/j.foodhyd.2018.06.011
   Web of Science ®Google Scholar
• Yang, Y., Li, D., & Xu, C. (2015). Influences of urea, pH and metal ions on the interaction between cepharanthine and lysozyme by steady state fluorescence spectroscopy. Journal of Molecular Structure, 1084, 229–235. doi:10.1016/j.molstruc.2014.12.060
   Web of Science ®Google Scholar
• Yu, J. E., Mallapaty, A., & Miller, R. L. (2018). It’s not just the food you eat: Environmental factors in the development of food allergies. Environmental Research, 165, 118–124. doi:10.1016/j.envres.2018.03.028
   PubMed Web of Science ®Google Scholar
• Zhou, S., Seo, S., Alli, I., & Chang, Y.-W. (2015). Interactions of caseins with phenolic acids found in chocolate. Food Research International, 74, 177–184. doi:10.1016/j.foodres.2015.05.006
   PubMed Web of Science ®Google Scholar