Interactions of chlorophyll-derived photosensitizers with human serum albumin are determined by the central metal ion

References

• ACD/ChemSketch, version 2.1. (2020). Advanced Chemistry Development, Inc. www.acdlabs.com.
   Google Scholar
• Ascenzi, P., Bocedi, A., Notari, S., Menegatti, E., & Fasano, M. (2005). Heme impairs allosterically drug binding to human serum albumin Sudlow's site I. Biochemical and Biophysical Research Communications, 334(2), 481–486. https://doi.org/10.1016/j.bbrc.2005.06.127
   PubMed Web of Science ®Google Scholar
• Barakat, C., & Patra, D. (2013). Combining time-resolved fluorescence with synchronous fluorescence spectroscopy to study bovine serum albumin-curcumin complex during unfolding and refolding processes. Luminescence, 28(2), 149–155. https://doi.org/10.1002/bio.2354
   PubMed Web of Science ®Google Scholar
• Baroni, S., Mattu, M., Vannini, A., Cipollone, R., Aime, S., Ascenzi, P., & Fasano, M. (2001). Effect of ibuprofen and warfarin on the allosteric properties of haem-human serum albumin: A spectroscopic study. European Journal of Biochemistry, 268(23), 6214–6220. https://doi.org/10.1046/j.0014-2956.2001.02569.x
   PubMedGoogle Scholar
• Batista, A. N. L., Batista, J. M., Ashton, L., Bolzani, V. S., Furlan, M., & Blanch, E. W. (2014). Investigation of DMSO-induced conformational transitions in human serum albumin using two-dimensional Raman optical activity spectroscopy. Chirality, 26(9), 497–501. https://doi.org/10.1002/chir.22351
   PubMed Web of Science ®Google Scholar
• BIOVIA. (2021). Discovery Studio Visualizer, version 2021. Dassault Systèmes.
   Google Scholar
• Bonnett, R. (2003). Metal complexes for photodynamic therapy. Comprehensive Coordination Chemistry II, 945–1003. https://doi.org/10.1016/B0-08-043748-6/09204-5.
   Google Scholar
• Buchler, J. W., Lay, K. L., Smith, P. D., Scheidt, W. R., Rupprecht, G. A., & Kenny, J. E. (1976). Metal complexes with tetrapyrrole ligands. Journal of Organometallic Chemistry., 110(1), 109–120. https://doi.org/10.1016/S0022-328X(00)90164-5
   Web of Science ®Google Scholar
• Carter, D. C., He, X. M., Munson, S. H., Twigg, P. D., Gernert, K. M., Broom, M. B., & Miller, T. Y. (1989). Three-dimensional structure of human serum albumin. Science (New York, N.Y.), 244(4909), 1195–1198. https://doi.org/10.1126/science.2727704
   PubMed Web of Science ®Google Scholar
• Chaves, O. A., de, A., Amorim, P. O., Castro, L. H. E., Sant’Anna, C. M. R., De Oliveira, M. C. C., Cesarin-Sobrinho, D., Netto-Ferreira, J. C., & Ferreira, A. B. B. (2015). Fluorescence and docking studies of the interaction between human serum albumin and pheophytin. Molecules (Basel, Switzerland), 20(10), 19526–19539. https://doi.org/10.3390/molecules201019526
   PubMed Web of Science ®Google Scholar
• Cui, F., Yan, Y., Zhang, Q., Du, J., Yao, X., Qu, G., & Lu, Y. (2009). Characterization of the interaction between 2'-deoxyuridine and human serum albumin . Carbohydrate Research, 344(5), 642–647. https://doi.org/10.1016/j.carres.2009.01.009
   PubMed Web of Science ®Google Scholar
• Fiedor, L., Kania, A., Myśliwa-Kurdziel, B., Orzeł, Ł., & Stochel, G. G. (2008). Understanding chlorophylls: Central magnesium ion and phytyl as structural determinants. Biochimica et Biophysica Acta, 1777(12), 1491–1500. https://doi.org/10.1016/j.bbabio.2008.09.005
   PubMed Web of Science ®Google Scholar
• Ge, F., Chen, C., Liu, D., Han, B., Xiong, X., & Zhao, S. (2010). Study on the interaction between theasinesin and human serum albumin by fluorescence spectroscopy. Journal of Luminescense, 130(1), 168–173. https://doi.org/10.1016/j.jlumin.2009.08.003
   Web of Science ®Google Scholar
• Ghisaidoobe, A. B. T., & Chung, S. J. (2014). Intrinsic Tryptophan fluorescence in the detection and analysis of proteins: A focus on Förster resonance energy transfer techniques. International Journal of Molecular Sciences, 15(12), 22518–22538. https://doi.org/10.3390/ijms151222518
   PubMed Web of Science ®Google Scholar
• Hartwich, G., Fiedor, L., Simonin, I., Cmiel, E., Schäfer, W., Noy, D., Scherz, A., & Scheer, H. (1998). Metal-substituted bacteriochlorophylls. 1. Preparation and influence of metal and coordination on spectra. Journal of the American Chemical Society, 120(15), 3675–3683. https://doi.org/10.1021/ja970874u
   Web of Science ®Google Scholar
• Hosainzadeh, A., Gharanfoli, M., Saberi, M. R., & Chamani, J. K. (2012). Probing the interaction of human serum albumin with bilirubin in the presence of aspirin by multi-spectroscopic, molecular modeling and zeta potential techniques: Insight on binary and ternary systems. Journal of Biomolecular Structure & Dynamics, 29(5), 1013–1050. https://doi.org/10.1080/073911012010525029
   PubMed Web of Science ®Google Scholar
• Hoober, J. K., Eggink, L. L., & Chen, M. (2007). Chlorophylls, ligands and assembly of light-harvesting complexes in chloroplasts. Photosynth Res, 94(2-3), 387–400. https://doi.org/10.1007/s11120-007-9181-1
   PubMed Web of Science ®Google Scholar
• Jahanban-Esfahlan, A., Davaran, S., Moosavi-Movahedi, A. A., & Dastmalchi, S. (2017). Investigating the interaction of juglone (5-hydroxy-1, 4-naphthoquinone) with serum albumins using spectroscopic and in silico methods. Journal of the Iranian Chemical Society, 14(7), 1527–1540. https://doi.org/10.1007/s13738-017-1094-0
   Web of Science ®Google Scholar
• Jahanban-Esfahlan, A., Panahi-Azar, 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. https://doi.org/10.1002/bip.22697
   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
• 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, 69–77. https://doi.org/10.31883/pjfns/133203
   Web of Science ®Google Scholar
• Jakubowska, M., Szczygieł, M., Michalczyk-Wetula, D., Susz, A., Stochel, G., Elas, M., Fiedor, L., & Urbanska, K. (2013). Zinc-pheophorbide a-highly efficient low-cost photosensitizer against human adenocarcinoma in cellular and animal models. Photodiagnosis and Photodynamic Therapy, 10(3), 266–277. https://doi.org/10.1016/j.pdpdt.2012.12.004
   PubMed Web of Science ®Google Scholar
• Kamal, J. K. A., & Behere, D. V. (2005). Binding of heme to human serum albumin: Steady-state fluorescence, circular dichroism and optical difference spectroscopic studies. Indian Journal of Biochemistry & Biophysics, 42(1), 7–12.
   PubMed Web of Science ®Google Scholar
• Kragh-Hansen, U., Chuang, V. T. G., & Otagiri, M. (2002). Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biological & Pharmaceutical Bulletin, 25(6), 695–704. https://doi.org/10.1248/bpb.25.695
   PubMed Web of Science ®Google Scholar
• Lakowicz, J. R. (2006). Principles of Fluorescence Spectroscopy. Springer. https://doi.org/10.1007/978-0-387-46312-4.
   Google Scholar
• Lu, Y., Berry, S. M., & Pfister, T. D. (2001). Engineering novel metalloproteins: Design of metal-binding sites into native protein scaffolds. Chemical Reviews, 101(10), 3047–3080. https://doi.org/10.1021/cr0000574
   PubMed Web of Science ®Google Scholar
• Mazière, J. C., Morlière, P., & Santus, R. (1991). New trends in photobiology. The role of the low density lipoprotein receptor pathway in the delivery of lipophilic photosensitizers in the photodynamic therapy of tumours. Journal of Photochemistry and Photobiology B: Biology, 8(4), 351–360. https://doi.org/10.1016/1011-1344(91)80111-T
   PubMed Web of Science ®Google Scholar
• Morris, G. M., Huey, R., Lindstrom, W., Sanner, M. F., Belew, R. K., Goodsell, D. S., & Olson, A. J. (2009). AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. Journal of Computational Chemistry, 30(16), 2785–2791. https://doi.org/10.1002/jcc.21256
   PubMed Web of Science ®Google Scholar
• Navalkele, P., Belgrave, K., Altinok, D., Bhambhani, K., Taub, J. W., & Wang, Z. J. (2016). Hypoalbuminemia associated with neuroblastoma: A single institution experience. Annals of Pediatrics and Child Health, 4, 1–5. https://www.jscimedcentral.com/Pediatrics/pediatrics-4-1115.pdf.
   Google Scholar
• Neese, F., Wennmohs, F., Becker, U., & Riplinger, C. (2020). The ORCA quantum chemistry program package. The Journal of Chemical Physics, 152(22), 224108. https://doi.org/10.1063/5.0004608
   PubMed Web of Science ®Google Scholar
• Nicoletti, F. P., Howes, B. D., Fittipaldi, M., Fanali, G., Fasano, M., Ascenzi, P., & Smulevich, G. (2008). Ibuprofen induces an allosteric conformational transition in the heme complex of human serum albumin with significant effects on heme ligation. Journal of the American Chemical Society, 130(35), 11677–11688. https://doi.org/10.1021/ja800966t
   PubMed Web of Science ®Google Scholar
• O'Boyle, N. M., Banck, M., James, C. A., Morley, C., Vandermeersch, T., & Hutchison, G. R. (2011). Open Babel: An open chemical toolbox. Journal of Cheminformatics, 3, 33–14. https://doi.org/10.1186/1758-2946-3-33.
   PubMed Web of Science ®Google Scholar
• Origin, Version (2021). OriginLab Corporation.
   Google Scholar
• Ouameur, A. A., Marty, R., Supe, E., & Tajmir-Riahi, H. A. (2005). Human serum albumin complexes with chlorophyll and chlorophyllin. Biopolymers, 77(3), 129–136. https://doi.org/10.1002/bip.20173
   PubMed Web of Science ®Google Scholar
• Poór, M., Li, Y., Kunsági-Máté, S., Petrik, J., Vladimir-Knežević, S., & Kőszegi, T. (2013). Molecular displacement of warfarin from human serum albumin by flavonoid aglycones. Journal of Luminescense., 142, 122–127. https://doi.org/10.1016/j.jlumin.2013.03.056
   Web of Science ®Google Scholar
• Roufegarinejad, L., Amarowicz, R., & Jahanban-Esfahlan, A. (2019). Characterizing the interaction between pyrogallol and human serum albumin by spectroscopic and molecular docking methods. Journal of Biomolecular Structure & Dynamics, 37(11), 2766–2775. https://doi.org/10.1080/07391102.2018.1496854
   PubMed Web of Science ®Google Scholar
• Schrödinger, LLC. (2010). The PyMOL Molecular Graphics System, Version 1.3. Schrödinger, LLC.
   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
• Sudlow, G., Birkett, D. J., & Wade, D. N. (1976). Further characterization of specific drug binding sites on human serum albumin. Molecular Pharmacology, 12(6), 1052–1061. http://molpharm.aspetjournals.org/content/11/6/824.abstract.
   PubMed Web of Science ®Google Scholar
• Sułkowski, L., Osuch, C., Matyja, M., & Matyja, A. (2020). Hematoporphyrin binding sites on human serum albumin. Archives of Medical Science-Civilization Diseases, 5(1), 1–7. https://doi.org/10.5114/amscd.2020.92722
   Google Scholar
• Sułkowski, L., Pawełczak, B., Chudzik, M., & Maciążek-Jurczyk, M. (2016). Characteristics of the protoporphyrin IX binding sites on human serum albumin using molecular docking. Molecules, 21(11), 1519. https://doi.org/10.3390/molecules21111519
   PubMed Web of Science ®Google Scholar
• Szafraniec, M. J., & Fiedor, L. (2021). One ring is not enough to rule them all. Albumin-dependent ABCG2-mediated transport of chlorophyll-derived photosensitizers. European Journal of Pharmaceutical Sciences, 167, 106001. https://doi.org/10.1016/j.ejps.2021.106001
   PubMed Web of Science ®Google Scholar
• Szczygieł, M., Boroń, B., Szczygieł, D., Szafraniec, M., Susz, A., Matuszak, Z., Urbańska, K., & Fiedor, L. (2014). Real-time non-invasive transdermal monitoring of photosensitizer level in vivo for pharmacokinetic studies and optimization of photodynamic therapy protocol. Journal of Analytical & Bioanalytical Techniques, 5, 227. https://doi.org/10.4172/2155-9872.1000227
   Google Scholar
• Szczygieł, M., Urbańska, K., Jurecka, P., Stawoska, I., Stochel, G., & Fiedor, L. (2008). Central metal determines pharmacokinetics of chlorophyll-derived xenobiotics. Journal of Medicinal Chemistry, 51(15), 4412–4418. https://doi.org/10.1021/jm7016368
   PubMed Web of Science ®Google Scholar
• Takaaki, F., Tokuda, S., Nakazawa, Y., Kurozumi, S., Obayashi, S., Yajima, R., & Shirabe, K. (2020). Implications of low serum albumin as a prognostic factor of long-term outcomes in patients with breast cancer. In Vivo (Vivo), 34(4), 2033–2036. https://doi.org/10.21873/invivo.12003
   PubMed Web of Science ®Google Scholar
• Zunszain, P. A., Ghuman, J., Komatsu, T., Tsuchida, E., & Curry, S. (2003). Crystal structural analysis of human serum albumin complexed with hemin and fatty acid. BMC Structural Biology, 3, 6. https://doi.org/10.1186/1472-6807-3-6
   PubMedGoogle Scholar