128
Views
2
CrossRef citations to date
0
Altmetric
Research Articles

Study on the Binding of Methylphenanthrene Isomers with Different Methylated Positions to Human Serum Albumin Employing Spectroscopic Techniques Combined with Molecular Docking

, , , &
Pages 2704-2722 | Received 31 Dec 2019, Accepted 30 Oct 2020, Published online: 27 Nov 2020

References

  • L. L. Zhang, L. Yang, Q. Y. Zhou, X. Zhang, W. L. Xing, Y. J. Wei, M. Hu, L. X. Zhao, A. Toriba, K. Hayakawa, et al. “Size Distribution of Particulate Polycyclic Aromatic Hydrocarbons in Fresh Combustion Smoke and Ambient Air: A Review,” Journal of Environmental Sciences (China) 88, (2020): 370–84.
  • P. Gerde, B. A. Muggenburg, M. Lundborg, and A. R. Dah, “The Rapid Alveolar Absorption of Diesel Soot-Adsorbed Benzo[a]Pyrene: Bioavailability, Metabolism and Dosimetry of an Inhaled Particle-Borne Carcinogen,” Carcinogenesis 22, no. 5 (2001): 741–9.
  • K. Sexton, J. J. Salinas, T. J. McDonald, R. M. Z. Gowen, R. P. Miller, J. B. McCormick, and S. P. Fisher-Hoch, “Polycyclic Aromatic Hydrocarbons in Maternal and Umbilical Cord Blood from Pregnant Hispanic Women Living in Brownsville, Texas,” International Journal of Environmental Research and Public Health 8, no. 8 (2011): 3365–79.
  • G. Sabbioni, and R. J. Turesky, “Biomonitoring Human Albumin Adducts: The past, the Present, and the Future,” Chemical Research in Toxicology 30, no. 1 (2017): 332–66.
  • Y. S. Chen, Y. F. Zhou, M. Chen, B. J. Xie, J. F. Yang, J. G. Chen, and Z. D. Sun, “Isorenieratene Interaction with Human Serum Albumin: Multi-Spectroscopic Analyses and Docking Simulation,” Food Chemistry 258, (2018): 393–9.
  • Y. Y. Yue, Z. Y. Wang, Z. X. Wang, Y. Y. Zhang, and J. M. Liu, “A Comparative Study of Binding Properties of Different Coumarin-Based Compounds with Human Serum Albumin,” Journal of Molecular Structure 1169, (2018): 75–80.
  • J. M. Liu, X. Y. Yan, Y. Y. Yue, and S. F. Zhao, “Investigation of the Interaction of Aurantio-Obtusin with Human Serum Albumin by Spectroscopic and Molecular Docking Methods,” Luminescence : The Journal of Biological and Chemical Luminescence 33, no. 1 (2018): 104–11.
  • S. Curry, “Lessons from the Crystallographic Analysis of Small Molecule Binding to Human Serum Albumin,” Drug Metabolism and Pharmacokinetics 24, no. 4 (2009): 342–57.
  • X. L. Wang, Q. Liu, W. J. Zhong, L. P. Yang, J. Yang, A. Covaci, and L. Y. Zhu, “Estimating Renal and Hepatic Clearance Rates of Organophosphate Esters in Humans: Impacts of Intrinsic Metabolism and Binding Affinity with Plasma Proteins,” Environment International 134, (2020): 105321.
  • J. Zhang, W. X. Chen, B. W. Tang, W. Zhang, L. F. Chen, Y. Duan, Y. X. Zhu, Y. X. Zhu, and Y. Zhang, “Interactions of 1-Hydroxypyrene with Bovine Serum Albumin: Insights from Multi-Spectroscopy, Docking and Molecular Dynamics Simulation Methods,” RSC Advances 6, no. 28 (2016): 23622–33.
  • G. Fanali, A. d. Masi, V. Trezza, M. Marino, M. Fasano, and P. Ascenzi, “Human Serum Albumin: From Bench to Bedside,” Molecular Aspects of Medicine 33, no. 3 (2012): 209–90.
  • K. Skupińska, M. Zylm, I. Misiewicz, and T. Kasprzycka-Guttman, “Interaction of Anthracene and Its Oxidative Derivatives with Human Serum Albumin,” A cta Biochimica Polonica 53, no. 1 (2006): 101–12.
  • T. Q. Wu, Q. Wu, S. Y. Guan, H. X. Su, and Z. J. Cai, “Binding of the Environmental Pollutant Naphthol to Bovine Serum Albumin,” Biomacromolecules 8, no. 6 (2007): 1899–906.
  • C. B. Xu, J. L. Gu, X. P. Ma, T. Dong, and X. L. Meng, “Investigation on the Interaction of Pyrene with Bovine Serum Albumin Using Spectroscopic Methods,” Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy 125, (2014): 391–5.
  • J. Zhang, L. F. Chen, D. Liu, Y. X. Zhu, and Y. Zhang, “Interactions of Pyrene and/or 1-Hydroxypyrene with Bovine Serum Albumin Based on EEM-PARAFAC Combined with Molecular Docking,” Talanta 186, (2018): 497–505.
  • R. Roy, R. Jan, G. Gunjal, R. Bhor, K. Pai, and P. G. Satsangi, “Particulate Matter Bound Polycyclic Aromatic Hydrocarbons: Toxicity and Health Risk Assessment of Exposed Inhabitants,” Atmospheric Environment 210, (2019): 47–57.
  • C. S. Casal, G. Arbilla, and S. M. Correa, “Alkyl Polycyclic Aromatic Hydrocarbons Emissions in Diesel/Biodiesel Exhaust,” Atmospheric Environment 96, (2014): 107–16.
  • H. K. Lin, G. D. Morandi, R. S. Brown, V. Snieckus, T. Rantanen, K. B. Jorgensen, and P. V. Hodson, “Quantitative Structure-Activity Relationships for Chronic Toxicity of Alkyl-Chrysenes and Alkyl-Benz[a]Anthracenes to Japanese Medaka Embryos (Oryziaslatipes),” Aquatic Toxicology 159, (2015): 109–18.
  • P. V. Hodson, “The Toxicity to Fish Embryos of PAH in Crude and Refined Oils,” Archives of Environmental Contamination and Toxicology 73, no. 1 (2017): 12–8.
  • S. Fallahtafti, T. Rantanen, R. S. Brown, V. Snieckus, and P. V. Hodson, “Toxicity of Hydroxylated Alkyl-Phenanthrenes to the Early Life Stages of Japanese Medaka (Oryziaslatipes),” Aquatic Toxicology 106-107, (2012): 56–64.
  • L. Wolińska, P. Brzuzan, M. Woeny, M. Gora, M. K. Luczyński, P. Podlasz, S. Kolwicz, and A. Piasecka, “Preliminary Study on Adverse Effects of Phenanthrene and Its Methyl and Phenyl Derivatives in Larval Zabrafish,” Daniorerio,” Environmental Biotechnology 7, no. 1 (2011): 26–33.
  • J. Zhang, “Study on the Interactions of Typical PAHs and Their Metabolites with Serum Albumin and Their Controlling Ways Using Cyclodextrins” (PhD diss., Xiamen University, 2016).
  • J. Vondrácek, L. Svihálková-Sindlerová, K. Pencíková, S. Marvanová, P. Krcmár, M. Ciganek, J. Neca, J. E. Trosko, B. Upham, A. Kozubík, et al. “Concentrations of Methylated Naphthalenes, Anthracenes, and Phenanthrenes Occurring in Czech River Sediments and Their Effects on Toxic Events Associated with Carcinogenesis in Rat Liver Cell Lines,” Environmental Toxicology and Chemistry 26, no. 11 (2007): 2308–16.
  • Y. Sun, I. I. I. C. A. Miller, Th. E. Wiese, and D. A. Blake, “Methylated Phenanthrenes Are More Potent than Phenanthrene in a Bioassay of Human Aryl Hydrocarbon Receptor (AhR) Signaling,” Environmental Toxicology and Chemistry 33, no. 10 (2014): 2363–7.
  • J. Zhang, L. F. Chen, Y. X. Zhu, and Y. Zhang, “Study on the Molecular Interactions of Hydroxylated Polycyclic Aromatic Hydrocarbons with Catalase Using Multi-Spectral Methods Combined with Molecular Docking,” Food Chemistry 309, (2020): 125743.
  • C. Han, S. B. Fang, H. M. Cao, Y. Lu, Y. Q. Ma, D. F. Wei, X. Y. Xie, X. H. Liu, X. Li, D. Q. Fei, et al. “Molecular Interaction of PCB153 to Human Serum Albumin: Insights from Spectroscopic and Molecular Modeling Studies,” Journal of Hazardous Materials 248–249, (2013): 313–21.
  • L. F. Chen, J. Zhang, Y. X. Zhu, and Y. Zhang, “Molecular Interaction of Inorganic Mercury(II) with Catalase: A Spectroscopic Study in Combination with Molecular Docking,” RSC Advances 5, no. 97 (2015): 79874–81.
  • H. T. Mu, S. H. Chen, F. Y. Liu, J. B. Xiao, H. Huang, Y. H. Zhang, Y. M. Sun, X. Y. Gao, H. T. Lei, and X. W. Yuan, “Stereoselective Interactions of Lactic Acid Enantiomers with HSA: Spectroscopy and Docking Application,” Food Chemistry 270, (2019): 429–35.
  • X. N. Xiong, R. X. Gan, Z. L. Suo, P. X. Tang, S. S. Zhang, Y. J. Zhu, Q. M. Sun, and H. Li, “Interactions between the Antiviral Drug Telaprevir and Human Serum Albumin: A Combined Study with Spectroscopic Methods and Molecular Modeling,” New Journal of Chemistry 42, no. 12 (2018): 9791–800.
  • M. M. Alam, F. A. Qais, I. Ahmad, P. Alam, R. H. Khan, and I. Naseem, “Multi-Spectroscopic and Molecular Modelling Approach to Investigate the Interaction of Riboflavin with Human Serum Albumin,” Journal of Biomolecular Structure & Dynamics 36, no. 3 (2018): 795–809.
  • F. Shen, Y. X. Liu, S. M. Li, C. K. Jiang, B. F. Wang, Y. H. Xiong, Z. W. Mao, and X. Y. Le, “Synthesis, Crystal Structures, Molecular Docking and in Vitro Cytotoxicity Studies of Two New Copper(II) Complexes: Special Emphasis on Their Binding to HSA,” New Journal of Chemistry 41, no. 21 (2017): 12429–41.
  • X. Y. Xie, W. J. Lü, and X. G. Chen, “Binding of the Endocrine Disruptors 4-Tert-Octylphenol and 4-Nonylphenol to Human Serum Albumin,” Journal of Hazardous Materials 248–249, (2013): 347–54.
  • Z. W. Wu, Z. S. Yi, L. Dong, and A. Q. Zhang, “Molecular Simulation Study of the Specific Combination between Four Kinds of Phthalic Acid Esters and Human Serum Albumin,” Environmental Toxicology and Pharmacology 41, (2016): 259–65.
  • S. Soares, N. Mateus, and V. D. Freitas, “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, no. 16 (2007): 6726–35. 
  • R Wang, X Hu, J. H. Pan, D. M. Gong, and G. W. Zhang, “Interaction between Quinoline Yellow and Human Serum Albumin: Spectroscopic, Chemometric and Molecular Docking Studies,” Journal of the Science of Food and Agriculture 99, no. 1 (2019): 73–82.
  • J. Równicka-Zubik, L. Sułkowski, and M. Toborek, “Interactions of PCBs with Human Serum Albumin: In Vitro Spectroscopic Study,” Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy 124, (2014): 632–7.
  • M. Maciążek-Jurczyk, A. Sułkowska, and J. Równicka-Zubik, “Alteration of Methotrexate Binding to Human Serum Albumin Induced by Oxidative Stress. Spectroscopic Comparative Study,” Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy 152, (2016): 537–50.
  • J. R. Lakowicz, eds., Principles of Fluorescence Spectroscopy, 3rd ed. (Baltimore, MD: Springer, 2006).
  • E. Rahnama, M. Mahmoodian-Moghaddam, S. Khorsand-Ahmadi, M. R. Saberi, and J. Chamani, “Binding Site Identification of Metformin to Human Serum Albumin and Glycated Human Serum Albumin by Spectroscopic and Molecular Modeling Techniques: A Comparison Study,” Journal of Biomolecular Structure & Dynamics 33, no. 3 (2015): 513–33.
  • R. Agrawal, Y. Thakur, M. Tripathi, M. K. Siddiqi, R. H. Khan, and R. Pande, “Elucidating the Binding Propensity of Naphthyl Hydroxamic Acid to Human Serum Albumin (HSA): Multi-Spectroscopic and Molecular Modeling Approach,” Journal of Molecular Structure 1184, (2019): 1–11.
  • M. Mondal, L. T. Pragna, R. Krishna, and N. Sakthivel, “Molecular Interaction between Human Serum Albumin (HSA) and Phloroglucinol Derivative That Shows Selective anti-Proliferative Potential,” Journal of Luminescence 192, (2017): 990–8.
  • A. S. Abdelhameed, A. H. Bakheit, H. K. AlRabiah, E. S. G. Hassan, and F. M. Almutairi, “Molecular Interactions of AL3818 (Anlotinib) to Human Serum Albumin as Revealed by Spectroscopic and Molecular Docking Studies,” Journal of Molecular Liquids 273, (2019): 259–65.
  • N. Maurya, J. K. Maurya, U. K. Singh, R. Dohare, M. Zafaryab, M. M. A. Rizvi, M. Kumari, and R. Patel, “In Vitro Cytotoxicity and Interaction of Noscapine with Human Serum Albumin: Effect on Structure and Esterase Activity of HSA,” Molecular Pharmaceutics 16, no. 3 (2019): 952–66.
  • Yuanyuan Yue, Shufang Zhao, Jianming Liu, Xuyang Yan, and Yangyang Sun, “Probing the Binding Properties of Dicyandiamide with Pepsin by Spectroscopy and Docking Methods,” Chemosphere 185, (2017): 1056–62.
  • Y. Y. Yue, Z. Y. Wang, Y. Y. Zhang, Z. X. Wang, Q. Z. Lü, and J. M. Liu, “Binding of Triclosan and Triclocarban to Pepsin: DFT, Spectroscopic and Dynamic Simulation Studies,” Chemosphere 214, (2019): 278–87.
  • M. Szczerba, and M. J. Rospondek, “Controls on Distributions of Methylphenanthrenes in Sedimentary Rock Extracts: Critical Evaluation of Existing Geochemical Data from Molecular Modelling,” Organic Geochemistry 41, no. 12 (2010): 1297–311.
  • Y. Z. Zhang, J. Zhang, F. F. Li, X. Xiang, A. Q. Ren, and Y. Liu, “Studies on the Interaction between Benzophenone and Bovine Serum Albumin by Spectroscopic Methods,” Molecular Biology Reports 38, no. 4 (2011): 2445–53.
  • G. F. Shen, T. T. Liu, Q. Wang, M. Jiang, and J. H. Shi, “Spectroscopic and Molecular Docking Studies of Binding Interaction of Gefitinib, Lapatinib and Sunitinib with Bovine Serum Albumin (BSA),” Journal of Photochemistry and Photobiology. B, Biology 153, (2015): 380–90.
  • A. S. Sharma, S. Anandakumar, and M. Ilanchelian, “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, (2014): 206–18.
  • M. Memarpoor-Yazdi, and H. Mahaki, “Probing the Interaction of Human Serum Albumin with Vitamin B2 (Riboflavin) and l-Arginine (l-Arg) Using Multi-Spectroscopic, Molecular Modeling and Zeta Potential Techniques,” Journal of Luminescence 136, (2013): 150–9.
  • J. B. Chen, X. F. Zhou, Y. L. Zhang, Y. J. Qian, and H. P. Gao, “Interactions of Acidic Pharmaceuticals with Human Serum Albumin: Insights into the Molecular Toxicity of Emerging Pollutants,” Amino Acids 43, no. 4 (2012): 1419–29.
  • X. Zhang, L. Chen, X. C. Fei, Y. S. Ma, and H. W. Gao, “Binding of PFOS to Serum Albumin and DNA: Insight into the Molecular Toxicity of Perfluorochemicals,” BMC Molecular Biology 10, (2009): 16.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.