Investigation into the site-specific binding interactions between chlorogenic acid and ovalbumin using multi-spectroscopic and in silico simulation studies

References

• Abdollahpour, N., Soheili, V., Saberi, M. R., & Chamani, J. (2016). Investigation of the interaction between human serum albumin and two drugs as binary and ternary systems. European Journal of Drug Metabolism and Pharmacokinetics, 41(6), 705–721. https://doi.org/10.1007/s13318-015-0297-y
   PubMed Web of Science ®Google Scholar
• Abdullah, S. M. S., Fatma, S., Rabbani, G., & Ashraf, J. M. A. (2017). Spectroscopic and molecular docking approach on the binding of tinzaparin sodium with human serum albumin. Journal of Molecular Structure, 1127, 283–288. https://doi.org/10.1016/j.molstruc.2016.07.108
   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(1), 520–531. https://doi.org/10.1021/jp208416d
   PubMed Web of Science ®Google Scholar
• Chen, X. (2019). A review on coffee leaves: Phytochemicals, bioactivities and applications. Critical Reviews in Food Science and Nutrition, 59(6), 1008–1025. https://doi.org/10.1080/10408398.2018.1546667
   PubMed Web of Science ®Google Scholar
• Chen, X.-M., Kitts, D. D., & Ma, Z. (2017). Demonstrating the relationship between the phytochemical profile of different teas with relative antioxidant and anti-inflammatory capacities. Functional Foods in Health and Disease, 7(6), 375–395. https://doi.org/10.31989/ffhd.v7i6.342
   Web of Science ®Google Scholar
• Dai, T., Chen, J., McClements, D. J., Hu, P., Ye, X., Liu, C., & Li, T. (2019). Protein-polyphenol interactions enhance the antioxidant capacity of phenolics: Analysis of rice glutelin-procyanidin dimer interactions. Food & Function, 10(2), 765–774. https://doi.org/10.1039/c8fo02246a
   PubMed Web of Science ®Google Scholar
• Dantas, M. D. D. A., de Araújo Tenório, H., Lopes, T. I. B., Pereira, H. J. V., Marsaioli, A. J., Figueiredo, I. M., & Santos, 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. https://doi.org/10.1016/j.ijbiomac.2017.04.052
   PubMed Web of Science ®Google Scholar
• Dehghani Sani, F., Shakibapour, N., Beigoli, S., Sadeghian, H., Hosainzadeh, M., & Chamani, J. (2018). Changes in binding affinity between ofloxacin and calf thymus DNA in the presence of histone H1: Spectroscopic and molecular modeling investigations. Journal of Luminescence, 203, 599–608. https://doi.org/10.1016/j.jlumin.2018.06.083
   Web of Science ®Google Scholar
• Dórea, J. G., & da Costa, T. H. M. (2005). Is coffee a functional food? British Journal of Nutrition, 93(6), 773–782. https://doi.org/10.1079/BJN20051370
   PubMed Web of Science ®Google Scholar
• Dzah, C. S., Duan, Y., Zhang, H., Wen, C., Zhang, J., Chen, G., & Ma, H. (2020). The effects of ultrasound assisted extraction on yield, antioxidant, anticancer and antimicrobial activity of polyphenol extracts: A review. Food Bioscience, 35, 100547–100556. https://doi.org/10.1016/j.fbio.2020.100547
   Web of Science ®Google Scholar
• Fu, X., Belwal, T., He, Y., Xu, Y., Li, L., & Luo, Z. (2020). Interaction and binding mechanism of cyanidin-3-O-glucoside to ovalbumin in varying pH conditions: A spectroscopic and molecular docking study. Food Chemistry, 320, 126616. https://doi.org/10.1016/j.foodchem.2020.126616
   PubMed Web of Science ®Google Scholar
• Gu, L., Peng, N., Chang, C., McClements, D. J., Su, Y., & Yang, Y. (2017). Fabrication of surface-active antioxidant food biopolymers: Conjugation of catechin polymers to egg white proteins. Food Biophysics, 12(2), 198–210. https://doi.org/10.1007/s11483-017-9476-5
   Web of Science ®Google Scholar
• He, D., Peng, X., Xing, Y.-F., Wang, Y., Zeng, W., Su, N., Zhang, C., Lu, D.-N., & Xing, X.-H. (2020). Increased stability and intracellular antioxidant activity of chlorogenic acid depend on its molecular interaction with wheat gluten hydrolysate. Food Chemistry, 325, 126873–126883. https://doi.org/10.1016/j.foodchem.2020.126873
   PubMed Web of Science ®Google Scholar
• Jia, J., Gao, X., Hao, M., & Tang, L. (2017). Comparison of binding interaction between β-lactoglobulin and three common polyphenols using multi-spectroscopy and modelling methods. Food Chemistry, 228, 143–151. https://doi.org/10.1016/j.foodchem.2017.01.131
   PubMed Web of Science ®Google Scholar
• Kamshad, M., Jahanshah Talab, M., Beigoli, S., Sharifirad, A., & Chamani, J. (2019). Use of spectroscopic and zeta potential techniques to study the interaction between lysozyme and curcumin in the presence of silver nanoparticles at different sizes. Journal of Biomolecular Structure and Dynamics, 37(8), 2030–2040. https://doi.org/10.1080/07391102.2018.1475258
   PubMed Web of Science ®Google Scholar
• Kang, J., Liu, Y., Xie, M.-X., Li, S., Jiang, M., & Wang, T.-D. (2004). Interactions of human serum albumin with chlorogenic acid and ferulic acid. Biochimica et Biophysica Acta (BBA) - General Subjects, 1674(2), 205–214. https://doi.org/10.1016/j.bbagen.2004.06.021
   PubMed Web of Science ®Google Scholar
• Kawachi, Y., Kameyama, R., Handa, A., Takahashi, N., & Tanaka, N. (2013). Role of the N-terminal amphiphilic region of ovalbumin during heat-induced aggregation and gelation. Journal of Agricultural and Food Chemistry, 61(36), 8668–8675. https://doi.org/10.1021/jf402456v
   PubMed Web of Science ®Google Scholar
• Lakowicz, J. R. (2006). Principles of fluorescence spectroscopy. Springer.
   Google Scholar
• Li, T., Hu, P., Dai, T., Li, P., Ye, X., Chen, J., & Liu, C. (2018). Comparing the binding interaction between β-lactoglobulin and flavonoids with different structure by multi-spectroscopy analysis and molecular docking. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 201, 197–206. https://doi.org/10.1016/j.saa.2018.05.011
   PubMed Web of Science ®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. https://doi.org/10.1007/s10895-016-1948-3
   PubMed Web of Science ®Google Scholar
• Li, X., Wang, G., Chen, D., & Lu, Y. (2015). β-Carotene and astaxanthin with human and bovine serum albumins. Food Chemistry, 179, 213–221. https://doi.org/10.1016/j.foodchem.2015.01.133
   PubMed Web of Science ®Google Scholar
• Lin, X., Li, W., Ye, C., & Liu, Z. (2015). Study on the mechanism of interaction between tubeimoside I and human serum albumin at different temperatures by three-dimensional fluorescence spectrum. International Journal of Thermophysics, 36(5–6), 919–923. https://doi.org/10.1007/s10765-014-1657-6
   Web of Science ®Google Scholar
• Liu, F., Sun, C., Yang, W., Yuan, F., & Gao, Y. (2015). Structural characterization and functional evaluation of lactoferrin–polyphenol conjugates formed by free-radical graft copolymerization. RSC Advances, 5(20), 15641–15651. https://doi.org/10.1039/C4RA10802G
   Web of Science ®Google Scholar
• Liu, G., Yuan, D., Wang, Q., Li, W., Cai, J., Li, S., Lamikanra, O., & Qin, X. J. (2018a). Maillard-reaction-functionalized egg ovalbumin stabilizes oil nanoemulsions. Journal of Agricultural and Food Chemistry, 66(16), 4251–4258. https://doi.org/10.1021/acs.jafc.8b00423
   PubMed Web of Science ®Google Scholar
• Liu, Y., Cai, Y., Ying, D., Fu, Y., Xiong, Y., & Le, X. (2018b). Ovalbumin as a carrier to significantly enhance the aqueous solubility and photostability of curcumin: Interaction and binding mechanism study. International Journal of Biological Macromolecules, 116, 893–900. https://doi.org/10.1016/j.ijbiomac.2018.05.089
   PubMed Web of Science ®Google Scholar
• Liu, Y., Ying, D., Cai, Y., & Le, X. (2017). Improved antioxidant activity and physicochemical properties of curcumin by adding ovalbumin and its structural characterization. Food Hydrocolloids, 72, 304–311. https://doi.org/10.1016/j.foodhyd.2017.06.007
   Web of Science ®Google Scholar
• Lu, Y., Li, S., Xu, H., Zhang, T., Lin, X., & Wu, X. (2018). Effect of covalent interaction with chlorogenic acid on the allergenic capacity of Ovalbumin. Journal of Agricultural and Food Chemistry, 66(37), 9794–9800. https://doi.org/10.1021/acs.jafc.8b03410
   PubMed Web of Science ®Google Scholar
• Ma, Z., Prasanna, G., Jiang, L., & Jing, P. (2020). Molecular interaction of cyanidin-3-O-glucoside with ovalbumin: Insights from spectroscopic, molecular docking and in vitro digestive studies. Journal of Biomolecular Structure & Dynamics, 38(6), 1858–1867. https://doi.org/10.1080/07391102.2019.1618735
   PubMed Web of Science ®Google Scholar
• Manivel, P., & Chen, X. (2020). Chlorogenic, caffeic, and ferulic acids and their derivatives in foods, handbook of dietary phytochemicals (pp. 1–31). Springer.
   Google Scholar
• Manivel, P., Anandakumar, S., & Ilanchelian, M. (2015). Exploring the interaction of the photodynamic therapeutic agent thionine with bovine serum albumin: Multispectroscopic and molecular docking studies. Luminescence, 30(6), 729–739. https://doi.org/10.1002/bio.2812
   PubMed Web of Science ®Google Scholar
• Manivel, P., Parthiban, M., & Ilanchelian, M. (2020). Exploring the binding mechanism between methylene blue and ovalbumin using spectroscopic analyses and computational simulations. Journal of Biomolecular Structure & Dynamics, 38(6), 1838–1847. https://doi.org/10.1080/07391102.2019.1618734
   PubMed Web of Science ®Google Scholar
• Mine, Y. (2007). Egg proteins and peptides in human health-chemistry, bioactivity and production. Current Pharmaceutical Design, 13(9), 875–884. https://doi.org/10.2174/138161207780414278
   PubMed Web of Science ®Google Scholar
• Mokaberi, P., Babayan-Mashhadi, F., Amiri Tehrani Zadeh, Z., Saberi, M. R., & Chamani, J. (2020). Analysis of the interaction behavior between Nano-Curcumin and two human serum proteins: Combining spectroscopy and molecular stimulation to understand protein-protein interaction. Journal of Biomolecular Structure and Dynamics. https://doi.org/10.1080/07391102.2020.1766570
   Google Scholar
• Mokaberi, P., Reyhani, V., Amiri-Tehranizadeh, Z., Saberi, M. R., Beigoli, S., Samandar, F., & Chamani, J. (2019). New insights into the binding behavior of lomefloxacin and human hemoglobin using biophysical techniques: Binary and ternary approaches. New Journal of Chemistry, 43(21), 8132–8145. https://doi.org/10.1039/C9NJ01048C
   Web of Science ®Google Scholar
• Moosavi-Movahedi, A. A., Chamani, J., Ghourchian, H., Shafiey, H., Sorenson, C. M., & Sheibani, N. (2003). Electrochemical evidence for the molten globule states of cytochrome c induced by N-alkyl sulfates at low concentrations. Journal of Protein Chemistry, 22(1), 23–30. https://doi.org/10.1023/a:1023011609931
   PubMedGoogle Scholar
• Moosavi-Movahedi, A. A., Golchin, A. R., Nazari, K., Chamani, J., Saboury, A. A., Bathaie, S. Z., & Tangestani-Nejad, S. (2004). Microcalorimetry, energetics and binding studies of DNA–dimethyltin dichloride complexes. Thermochimica Acta, 414(2), 233–241. https://doi.org/10.1016/j.tca.2004.01.007
   Web of Science ®Google Scholar
• Ozdal, T., Capanoglu, E., & Altay, F. (2013). A review on protein–phenolic interactions and associated changes. Food Research International, 51(2), 954–970. https://doi.org/10.1016/j.foodres.2013.02.009
   Web of Science ®Google Scholar
• Rajamanikandan, R., Selva Sharma, A., & Ilanchelian, M. (2019). New insights into the binding interaction of food protein ovalbumin with malachite green dye by hybrid spectroscopic and molecular docking analysis. Journal of Biomolecular Structure & Dynamics, 37(16), 4292–4300. https://doi.org/10.1080/07391102.2018.1550441
   PubMed Web of Science ®Google Scholar
• Rashidipour, S., Naeeminejad, S., & Chamani, J. (2016). Study of the interaction between DNP and DIDS with human hemoglobin as binary and ternary systems: Spectroscopic and molecular modeling investigation. Journal of Biomolecular Structure & Dynamics, 34(1), 57–77. https://doi.org/10.1080/07391102.2015.1009946
   PubMed Web of Science ®Google Scholar
• Rawel, H. M., Rohn, S., Kruse, H.-P., & Kroll, J. (2002). Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid. Food Chemistry, 78(4), 443–455. https://doi.org/10.1016/S0308-8146(02)00155-3
   Web of Science ®Google Scholar
• Sadeghzadeh, F., Entezari, A. A., Behzadian, K., Habibi, K., Amiri-Tehranizadeh, Z., Asoodeh, A., Saberi, M. R., & Chamani, J. (2020). Characterizing the binding of angiotensin converting enzyme I inhibitory peptide to human hemoglobin: Influence of electromagnetic fields. Protein and Peptide Letters, 27(10), 1007–1021. https://doi.org/10.2174/1871530320666200425203636
   PubMed Web of Science ®Google Scholar
• Shakibapour, N., Dehghani Sani, F., Beigoli, S., Sadeghian, H., & Chamani, J. (2019). Multi-spectroscopic and molecular modeling studies to reveal the interaction between propyl acridone and calf thymus DNA in the presence of histone H1: Binary and ternary approaches. Journal of Biomolecular Structure and Dynamics, 37(2), 359–371. https://doi.org/10.1080/07391102.2018.1427629
   PubMed Web of Science ®Google Scholar
• Shan, Y., Klepeis, J. L., Eastwood, M. P., Dror, R. O., & Shaw, D. E. (2005). Gaussian split Ewald: A fast Ewald mesh method for molecular simulation. The Journal of Chemical Physics, 122(5), 54101. https://doi.org/10.1063/1.1839571
   PubMed Web of Science ®Google Scholar
• Shanmugaraj, K., Umadevi, P., Senthilkumar, L., & Ilanchelian, M. (2017). Elucidation of binding mechanism of photodynamic therapeutic agent toluidine blue O with chicken egg white lysozyme by spectroscopic and molecular dynamics studies. Photochemistry and Photobiology, 93(4), 1043–1056. https://doi.org/10.1111/php.12744
   PubMed Web of Science ®Google Scholar
• Sharifi-Rad, A., Mehrzad, J., Darroudi, M., Saberi, M. R., & Chamani, J. (2020). Oil-in-water nanoemulsions comprising Berberine in olive oil: Biological activities, binding mechanisms to human serum albumin or holo-transferrin and QMMD simulations. Journal of Biomolecular Structure and Dynamics, 39(3), 1029-1043. https://doi.org/10.1080/07391102.2020.1724568
   Google Scholar
• Sharma, A. S., Viswadevarayalu, A., Bharathi, A. C., Anand, K., Ali, S., Li, H., Ibrahim, B. S., & Chen, Q. (2020). Unravelling the distinctive mode of cooperative and independent interaction mechanism of 1-butyl-2, 3-dimethylimidazolium tetrafluoroborate ionic liquid with model transport proteins by comprehensive spectroscopic and computational studies. Journal of Molecular Structure, 1205, 127591–127601. https://doi.org/10.1016/j.molstruc.2019.127591
   Web of Science ®Google Scholar
• Shi, X., Zhang, T., Li, X., Feng, Y., Tan, X., & Jin, Y. (2016). Interaction between tangeretin and ovalbumin to reduce the allergic effects of Ovalbumin. Chemical Research in Chinese Universities, 32(4), 556–560. https://doi.org/10.1007/s40242-016-6016-7
   Web of Science ®Google Scholar
• Sinisi, V., Forzato, C., Cefarin, N., Navarini, L., & Berti, F. (2015). Interaction of chlorogenic acids and quinides from coffee with human serum albumin. Food Chemistry, 168, 332–340. https://doi.org/10.1016/j.foodchem.2014.07.080
   PubMed Web of Science ®Google Scholar
• Sohrabi, T., Hosseinzadeh, M., Beigoli, S., Saberi, M. R., & Chamani, J. (2018). Probing the binding of lomefloxacin to a calf thymus DNA-histone H1 complex by multi-spectroscopic and molecular modeling techniques. Journal of Molecular Liquids, 256, 127–138. https://doi.org/10.1016/j.molliq.2018.02.031
   Web of Science ®Google Scholar
• Spizzirri, U. G., Iemma, F., Puoci, F., Cirillo, G., Curcio, M., Parisi, O. I., & Picci, N. (2009). Synthesis of antioxidant polymers by grafting of gallic acid and catechin on gelatine. Biomacromolecules, 10(7), 1923–1930. https://doi.org/10.1021/bm900325t
   PubMed Web of Science ®Google Scholar
• Su, M., Liu, F., Luo, Z., Wu, H., Zhang, X., Wang, D., Zhu, Y., Sun, Z., Xu, W., & Miao, Y. (2019). The antibacterial activity and mechanism of chlorogenic acid against foodborne pathogen Pseudomonas aeruginosa. Foodborne Pathogens and Disease, 16(12), 823–830. https://doi.org/10.1089/fpd.2019.2678
   PubMed Web of Science ®Google Scholar
• Tang, B., Huang, Y., Ma, X., Liao, X., Wang, Q., Xiong, X., & Li, H. (2016). Multispectroscopic and docking studies on the binding of chlorogenic acid isomers to human serum albumin: Effects of esteryl position on affinity. Food Chemistry, 212, 434–442. https://doi.org/10.1016/j.foodchem.2016.06.007
   PubMed Web of Science ®Google Scholar
• Tanzadehpanah, H., Asoodeh, A., Saberi, M. R., & Chamani, J. (2013). Identification of a novel angiotensin-I converting enzyme inhibitory peptide from ostrich egg white and studying its interactions with the enzyme. Innovative Food Science & Emerging Technologies, 18, 212–219. https://doi.org/10.1016/j.ifset.2013.02.002
   Web of Science ®Google Scholar
• Vardevanyan, P. O., Antonyan, A. P., Parsadanyan, M. A., Shahinyan, M. A., & Mikaelyan, M. S. (2019). Study of Methylene Blue Interaction with Human Serum Albumin. Biophysical Reviews and Letters, 14(01), 17–25. https://doi.org/10.1142/S1793048019500012
   Google Scholar
• Walle, T. (2004). Absorption and metabolism of flavonoids. Free Radical Biology & Medicine, 36(7), 829–837. https://doi.org/10.1016/j.freeradbiomed.2004.01.002
   PubMed Web of Science ®Google Scholar
• Wang, D., Zhang, M., Wang, T., Cai, M., Qian, F., Sun, Y., & Wang, Y. (2019). Green tea polyphenols prevent lipopolysaccharide-induced inflammatory liver injury in mice by inhibiting NLRP3 inflammasome activation. Food & Function, 10(7), 3898–3908. https://doi.org/10.1039/c9fo00572b
   PubMed Web of Science ®Google Scholar
• Wang, J., Dadmohammadi, Y., Jaiswal, A., & Abbaspourrad, A. J. (2020). Investigation of the interaction between N-acetyl-L-cysteine and ovalbumin by spectroscopic studies, molecular docking simulation, and real-time quartz crystal microbalance with dissipation. Journal of Agricultural and Food Chemistry, 68(37), 10184–10190. https://doi.org/10.1021/acs.jafc.0c03201
   PubMed Web of Science ®Google Scholar
• Wang, Y., Zhao, L., Wang, C., Hu, J., Guo, X., Zhang, D., Wu, W., Zhou, F., & Ji, B. (2017). Protective effect of quercetin and chlorogenic acid, two polyphenols widely present in edible plant varieties, on visible light-induced retinal degeneration in vivo. Journal of Functional Foods, 33, 103–111. https://doi.org/10.1016/j.jff.2017.02.034
   Web of Science ®Google Scholar
• Wianowska, D., & Gil, M. (2019). Recent advances in extraction and analysis procedures of natural chlorogenic acids. Phytochemistry Reviews, 18(1), 273–302. https://doi.org/10.1007/s11101-018-9592-y
   Web of Science ®Google Scholar
• Yamasaki, M., Takahashi, N., & Hirose, M. (2003). Crystal structure of S-ovalbumin as a non-loop-inserted thermostabilized serpin form. The Journal of Biological Chemistry, 278(37), 35524–35530. https://doi.org/10.1074/jbc.M305926200
   PubMed Web of Science ®Google Scholar
• Yang, W., Tu, Z., Wang, H., Zhang, L., & Song, Q. (2018). Glycation of ovalbumin after high-intensity ultrasound pretreatment: Effects on conformation, immunoglobulin (Ig)G/IgE binding ability and antioxidant activity. Journal of the Science of Food and Agriculture, 98(10), 3767–3773. https://doi.org/10.1002/jsfa.8890
   PubMed Web of Science ®Google Scholar