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Research Articles

Probing the interaction of fisetin with human serum transferrin via spectroscopic and molecular docking approaches

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Pages 9613-9619 | Received 13 Apr 2021, Accepted 15 May 2021, Published online: 07 Jun 2021

References

  • BIOVIA - Dassault Systèmes, [Discovery Studio], (2021). Dassault Systèmes.
  • Byrne, S. (2009) Investigation of the molecular basis of receptor mediated iron release from transferrin [Graduate College, Dissertations and Theses, 38].
  • Chilom, C. G., Bacalum, M., Stanescu, M. M., & Florescu, M. (2018). Insight into the interaction of human serum albumin with folic acid: A biophysical study. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 204, 648–656. https://doi.org/10.1016/j.saa.2018.06.093
  • Chilom, C. G., Bălan, A., Sandu, N., Bălăşoiu, M., Stolyar, S., & Orelovich, O. (2020). Exploring the conformation and thermal stability of human serum albumin corona of ferrihydrite nanoparticles. International Journal of Molecular Sciences, 21(24), 9734. https://doi.org/10.3390/ijms21249734
  • Dallakyan, S., & Olson, A. J. (2015). Small-molecule library screening by docking with PyRx. Methods in Molecular Biology (Clifton, N.J.), 1263, 243–250. https://doi.org/10.1007/978-1-4939-2269-7_19
  • Eckenroth, B. E., Steere, A. N., Chasteen, N. D., Everse, S. J., & Mason, A. B. (2011). How the binding of human transferrin primes the transferrin receptor potentiating iron release at endosomal pH. Proceedings of the National Academy of Sciences of the United States of America, 108(32), 13089–13094. https://doi.org/10.1073/pnas.1105786108
  • He, Q. Y., Mason, A. B., Lyons, B. A., Tam, B. M., Nguyen, V., MacGillivray, R. T., & Woodworth, R. C. (2001). Spectral and metal-binding properties of three single-point tryptophan mutants of the human transferrin N-lobe, The. Biochemical Journal, 354(2), 423–429. https://doi.org/10.1042/0264-6021:3540423
  • https://pubchem.ncbi.nlm.nih.gov/compound/Fisetin
  • Jahanban-Esfahlan, J. A., Azar, P. V., & Sajedi, S. (2015). Spectroscopic and molecular docking studies on the interaction between N-acetyl cysteine and bovine serum albumin. Biopolymers, 103(11), 638–645. 10.1002/bip.22697 https://doi.org/10.1002/bip.22697
  • Jahanban-Esfahlan, A., Roufegarinejad, L., Tabibiazar, M., Lorenzo, J. M., & Amarowicz, R. (2021). Exploring the interactions between caffeic acid and human serum albumin using spectroscopic and molecular docking techniques. Polish Journal of Food and Nutrition Sciences, 71(1), 69–77. 10.31883/pjfns/133203.
  • James, N. G., Ross, J. A., Mason, A. B., & Jameson, D. M. (2010). Excited-state lifetime studies of the three tryptophan residues in the N-lobe of human serum transferrin. Protein Science: A Publication of the Protein Society, 19(1), 99–110. https://doi.org/10.1002/pro.287
  • Kim, S., Chen, J., Cheng, T., Gindulyte, A., He, J., He, S., Li, O., Shoemaker, B. A., Thiessen, P. A., Yu, B., Zaslavsky, L., Zhang, J., & Bolton, E. E. (2019). PubChem 2019 update: Improved access to chemical data. Nucleic Acids Research., 47, 1102–1109. https://doi.org/10.1093/nar/gky1033
  • Lakowicz, R. (2007). Principles of Fluorescence Spectroscopy (pp. 443–475), Plenum Press.
  • Li, D., Zhang, T., Xu, C., & Ji, B. (2011). Effect of pH on the interaction of vitamin B12 with bovine serum albumin by spectroscopic approaches. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 83(1), 598–608. https://doi.org/10.1016/j.saa.2011.09.012.
  • MacGillivray, R. T., Mendez, E., Shewale, J. G., Sinha, S. K., Lineback-Zins, J., & Brew, K. (1983). The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure. The Journal of Biological Chemistry, 258(6), 3543–3553.
  • Maher, P. (2006). A comparison of the neurotrophic activities of the flavonoid fisetin and some of its derivatives. Free Radical Research, 40(10), 1105–1111. https://doi.org/10.1080/10715760600672509
  • National Center for Biotechnology Information (2021). PubChem compound summary for CID 5281614, Fisetin. Retrieved March 21, 2021 from https://pubchem.ncbi.nlm.nih.gov/compound/Fisetin.
  • Panche, A. N., Diwan, A. D., & Chandra, S. R. (2016). Flavonoids: An overview. Journal of Nutritional Science, 5, E47. https://doi.org/10.1017/jns.2016.41
  • 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. https://doi.org/10.1002/jcc.20084
  • RCSB PDB: www.rcsb.org/structure/1D3K
  • Sandu, N., Chilom, C. G., & Popescu, A. I. (2021). Structural and molecular aspects of flavonoids as ligands for serum transferrin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 254, 119600. https://doi.org/10.1016/j.saa.2021.119600
  • Shukla, R., Pandey, V., Vadnere, G. P., & Lodhi, S. (2019). Role of flavonoids in management of inflammatory disorders, bioactive food as dietary interventions for arthritis and related inflammatory diseases (2nd ed., pp. 293–322). Academic Press. https://doi.org/10.1016/B978-0-12-813820-5.00018-0.
  • Trott, O., & Olson, A. J. (2010). AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. Journal of Computational Chemistry, 31(2), 455–461. https://doi.org/10.1002/jcc.21334
  • Vahedian Movahed, H., Saberi, M. R., & Chamani, J. (2011). Comparison of binding interactions of lomefloxacin to serum albumin and serum transferrin by resonance light scattering and fluorescence quenching methods. Journal of Biomolecular Structure & Dynamics, 28(4), 483–502. https://doi.org/10.1080/07391102.2011.10508590
  • Wally, J., & Buchanan, S. K. (2007). A structural comparison of human serum transferrin and human lactoferrin. Biometals: An International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine, 20(3-4), 249–262. https://doi.org/10.1007/s10534-006-9062-7
  • Yang, A. H., MacGillivray, R. T., Chen, J., Luo, Y., Wang, Y., Brayer, G. D., Mason, A. B., Woodworth, R. C., & Murphy, M. E. (2000). Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron. Protein Science: A Publication of the Protein Society, 9(1), 49–52. https://doi.org/10.1110/ps.9.1.49
  • Yang, N., Zhang, H., Wang, M., Hao, Q., & Sun, H. (2012). Iron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe. Scientific Reports, 2(1), 999. https://doi.org/10.1038/srep00999

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