Spectroscopic and molecular docking investigation on the interaction of a water-soluble Cu(II) complex containing diethanolamine and dipicolinic acid ligands with human serum albumin

References

• Bagheri, M., & Fatemi, M. H. (2018). Fluorescence spectroscopy, molecular docking and molecular dynamic simulation studies of HSA-Aflatoxin B1 and G1 interactions. Journal of Luminescence, 202, 345–353. https://doi.org/10.1016/j.jlumin.2018.05.066
   Web of Science ®Google Scholar
• Blockhuys, S., Celauro, E., Hildesjö, C., Feizi, A., Stål, O., Fierro-González, J., & Wittung-Stafshede, P. (2017). Defining the human copper proteome and analysis of its expression variation in cancers. Metallomics: Integrated Biometal Science, 9(2), 112–123. https://doi.org/10.1039/c6mt00202a
   PubMed Web of Science ®Google Scholar
• Esmaeilzadeh, J., Mardani Z., Golsanamlou, V., Moeini K., & Kerautscheid, H. (2021). Evaluation of biological activities of cobalt(II) and copper(II) complexes synthesized from methylcarboxylate and amino alcohol ligand mixtures: spectroscopic, structural and docking studies. Inorg. Nanomet. Chem., https://doi.org/10.1080/24701556.2021.1980033
   Google Scholar
• Gawali, I. T., & Usmani, G. A. (2020). Novel non-ionic gemini surfactants from fatty acid and diethanolamine: Synthesis, surface-active properties and anticorrosion study. Chemistry Africa, 3(1), 75–88. https://doi.org/10.1007/s42250-019-00107-5
   Google Scholar
• He, X. M., & Carter, D. C. (1992). Atomic structure and chemistry of human serum albumin. Nature, 358(6383), 209–215. https://doi.org/10.1038/358209a0
   PubMed Web of Science ®Google Scholar
• Holz, R. C., Bradshaw, J. M., & Bennett, B. (1998). Synthesis, molecular structure, and reactivity of dinuclear copper (II) complexes with carboxylate-rich coordination environments. Inorganic Chemistry, 37(6), 1219–1225. https://doi.org/10.1021/ic9707873
   PubMed Web of Science ®Google Scholar
• İnci, D., Aydın, R., Huriyet, H., Zorlu, Y., & Çinkılıç, N. (2018). Newly synthesized Cu (II) pyrazino [2, 3‐f][1, 10] phenanthroline complexes as potential anticancer candidates. Applied Organometallic Chemistry, 32(4), e4309. https://doi.org/10.1002/aoc.4309
   Web of Science ®Google Scholar
• İnci, D., Aydın, R., Vatan, Ö., Huriyet, H., Zorlu, Y., Çoşut, B., & Çinkılıç, N. (2019). Cu (II) tyrosinate complexes containing methyl substituted phenanthrolines: Synthesis, X‐ray crystal structures, biomolecular interactions, antioxidant activity, ROS generation and cytotoxicity. Applied Organometallic Chemistry, 33(1), e4652. https://doi.org/10.1002/aoc.4652
   Web of Science ®Google Scholar
• İnci, D., Aydın, R., Vatan, Ö., Sevgi, T., Yılmaz, D., Zorlu, Y., Yerli, Y., Çoşut, B., Demirkan, E., & Çinkılıç, N. (2017). Synthesis and crystal structures of novel copper (II) complexes with glycine and substituted phenanthrolines: Reactivity towards DNA/BSA and in vitro cytotoxic and antimicrobial evaluation. Journal of Biological Inorganic Chemistry: JBIC: A Publication of the Society of Biological Inorganic Chemistry, 22(1), 61–85. https://doi.org/10.1007/s00775-016-1408-1
   PubMed Web of Science ®Google Scholar
• İnci, D., Köseler, A., Zeytünlüoğlu, A., Aydın, R., & Zorlu, Y. (2019). Interaction of a new copper (II) complex by bovine serum albumin and dipeptidyl peptidase-IV. Journal of Molecular Structure, 1177, 317–322. https://doi.org/10.1016/j.molstruc.2018.09.086
   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. (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., 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., Roufegarinejad, L., Tabibiazar, M., Lorenzo, J., & 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
• Karadag, A., Yilmaz, V. T., & Thoene, C. (2001). Di-and triethanolamine complexes of Co (II), Ni (II), Cu (II) and Zn (II) with thiocyanate: Synthesis, spectral and thermal studies. Crystal structure of dimeric Cu (II) complex with deprotonated diethanolamine,[Cu2 (μ-dea) 2 (NCS) 2. Polyhedron, 20(7–8), 635–641. https://doi.org/10.1016/S0277-5387(01)00720-3
   Web of Science ®Google Scholar
• Kholeif, S., & Anderegg, G. (1999). Stability constant determinations of alitame with H (I) and Cu (II) under physiological conditions using potentiometric measurements. Food Chemistry, 64(3), 397–401. https://doi.org/10.1016/S0308-8146(98)00147-2
   Web of Science ®Google Scholar
• Kou, S. B., Lin, Z. Y., Wang, B. L., Shi, J. H., & Liu, Y. X. (2021). Evaluation of the binding behavior of olmutinib (HM61713) with model transport protein: Insights from spectroscopic and molecular docking studies. Journal of Molecular Structure, 1224, 129024. https://doi.org/10.1016/j.molstruc.2020.129024
   Web of Science ®Google Scholar
• Lakowicz, J., Spectroscopy, P. O F., & Edition, T. (2006). Principles of fluorescence spectroscopy. Springer Publications.
   Google Scholar
• Li, S., Cao, Y., & Geng, F. (2017). Genome-wide identification and comparative analysis of albumin family in vertebrates. Evolutionary Bioinformatics Online, 13, 1176934317716089. https://doi.org/10.1177/1176934317716089
   Web of Science ®Google Scholar
• Melillo, G., Cox, G. W., Radzioch, D., & Varesio, L. (1993). Picolinic acid, a catabolite of L-tryptophan, is a costimulus for the induction of reactive nitrogen intermediate production in murine macrophages. Journal of Immunology (Baltimore, MD: 1950), 150(9), 4031–4040. https://doi.org/10.4049/jimmunol.150.9.4031
   PubMed Web of Science ®Google Scholar
• Naji, S. Z., & Abd, A. A. (2019). Sensitivity analysis of using diethanolamine instead of methyldiethanolamine solution for GASCO’S Habshan acid gases removal plant. Frontiers in Energy, 13(2), 317–324. https://doi.org/10.1007/s11708-019-0622-2
   Web of Science ®Google Scholar
• Ni, Y., Liu, G., & Kokot, S. (2008). Fluorescence spectrometric study on the interactions of Isoprocarb and sodium 2-isopropylphenate with bovine serum albumin. Talanta, 76(3), 513–521. https://doi.org/10.1016/j.talanta.2008.03.037
   PubMed Web of Science ®Google Scholar
• Qian, J., Sun, M. M., Liu, M., & Gu, W. (2019). Macromolecular probe based on a NiII/TbIII coordination polymer for sensitive recognition of human serum albumin (HSA) and MnO4. –ACS Omega, 4(7), 11949–11959. https://doi.org/10.1021/acsomega.8b03326
   PubMed Web of Science ®Google Scholar
• Rabbani, G., Baig, M. H., Lee, E. J., Cho, W. K., Ma, J. Y., & Choi, I. (2017). Biophysical study on the interaction between eperisone hydrochloride and human serum albumin using spectroscopic, calorimetric, and molecular docking analyses. Molecular Pharmaceutics, 14(5), 1656–1665. https://doi.org/10.1021/acs.molpharmaceut.6b01124
   PubMed Web of Science ®Google Scholar
• Rasoulzadeh, F., Asgari, D., Naseri, A., & Rashidi, M. R. (2010). Spectroscopic studies on the interaction between erlotinib hydrochloride and bovine serum albumin. Daru: Journal of Faculty of Pharmacy, Tehran University of Medical Sciences, 18(3), 179–184. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3304362/
   PubMed Web of Science ®Google Scholar
• Ross, P. D., & Subramanian, S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20(11), 3096–3102. https://doi.org/10.1021/bi00514a017
   PubMed 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
• Safarnejad, A., Shaghaghi, M., Dehghan, G., & Soltani, S. (2016). Binding of carvedilol to serum albumins investigated by multi-spectroscopic and molecular modeling methods. Journal of Luminescence, 176, 149–158. https://doi.org/10.1016/j.jlumin.2016.02.001
   Web of Science ®Google Scholar
• Shahabadi, N., Hadidi, S., & Feizi, F. (2015). Study on the interaction of antiviral drug ‘Tenofovir’with human serum albumin by spectral and molecular modeling methods. Spectrochimica Acta Part A, Molecular and Biomolecular Spectroscopy, 138, 169–175. https://doi.org/10.1016/j.saa.2014.10.070
   PubMed Web of Science ®Google Scholar
• Shi, J. H., Pan, D. Q., Jiang, M., Liu, T. T., & Wang, Q. (2017). In vitro study on binding interaction of quinapril with bovine serum albumin (BSA) using multi-spectroscopic and molecular docking methods. Journal of Biomolecular Structure & Dynamics, 35(10), 2211–2223. https://doi.org/10.1080/07391102.2016.1213663
   PubMed Web of Science ®Google Scholar
• Shi, J. H., Wang, Q., Pan, D. Q., Liu, T. T., & Jiang, M. (2017). Characterization of interactions of simvastatin, pravastatin, fluvastatin, and pitavastatin with bovine serum albumin: Multiple spectroscopic and molecular docking. Journal of Biomolecular Structure & Dynamics, 35(7), 1529–1546. https://doi.org/10.1080/07391102.2016.1188416
   PubMed Web of Science ®Google Scholar
• Siddiqi, Z. A., Khalid, M., Kumar, S., Shahid, M., & Noor, S. (2010). Antimicrobial and SOD activities of novel transition metal complexes of pyridine-2, 6-dicarboxylic acid containing 4-picoline as auxiliary ligand. European Journal of Medicinal Chemistry, 45(1), 264–269. https://doi.org/10.1016/j.ejmech.2009.10.005
   PubMed Web of Science ®Google Scholar
• Singh, M. R., Bhrara, K., & Singh, G. (2007). The inhibitory effect of diethanolamine on corrosion of mild steel in 0.5 M sulphuric acidic medium. Portugaliae Electrochimica Acta, 26(6), 479–492. https://doi.org/10.4152/pea.200806479
   Google Scholar
• Slieman, T. A., & Nicholson, W. L. (2001). Role of dipicolinic acid in survival of Bacillus subtilis spores exposed to artificial and solar UV radiation. Applied and Environmental Microbiology, 67(3), 1274–1279. https://doi.org/10.1128/AEM.67.3.1274-1279.2001
   PubMed Web of Science ®Google Scholar
• Sułkowska, A. (2002). Interaction of drugs with bovine and human serum albumin. Journal of Molecular Structure, 614(1–3), 227–232. https://doi.org/10.1016/S0022-2860(02)00256-9
   Web of Science ®Google Scholar
• Tauler, R., Casassas, E., & Rode, B. (1986). The complex formation of Cu (II) with mono-and di-ethanolamine in aqueous solution. Inorganica Chimica Acta, 114(2), 203–209. https://doi.org/10.1016/S0020-1693(00)86455-5
   Web of Science ®Google Scholar
• Vonk, W. I., Wijmenga, C., & van de Sluis, B. (2008). Relevance of animal models for understanding mammalian copper homeostasis. The American Journal of Clinical Nutrition, 88(3), 840S–845S. https://doi.org/10.1093/ajcn/88.3.840S
   PubMed Web of Science ®Google Scholar
• Wang, Y. Q., Tang, B. P., Zhang, H. M., Zhou, Q. H., & Zhang, G. C. (2009). Studies on the interaction between imidacloprid and human serum albumin: Spectroscopic approach. Journal of Photochemistry and Photobiology. B, Biology, 94(3), 183–190. https://doi.org/10.1016/j.jphotobiol.2008.11.013
   PubMed Web of Science ®Google Scholar
• Wang, Y., Wang, X., Wang, J., Zhao, Y., He, W., & Guo, Z. (2011). Noncovalent interactions between a trinuclear monofunctional platinum complex and human serum albumin. Inorganic Chemistry, 50(24), 12661–12668. https://doi.org/10.1021/ic201712e
   PubMed Web of Science ®Google Scholar
• Weder, J. E., Dillon, C. T., Hambley, T. W., Kennedy, B. J., Lay, P. A., Biffin, J., Regtop, H. L., & Davies, N. M. (2002). Copper complexes of non-steroidal anti-inflammatory drugs: An opportunity yet to be realized. Coordination Chemistry Reviews, 232(1–2), 95–126. https://doi.org/10.1016/S0010-8545(02)00086-3
   Web of Science ®Google Scholar
• Xu, A., Xu, F., Wang, W., Liu, W., & Song, Z. (2021). Effect of diethanolamine as corrosion inhibitor for the chemical mechanical polishing of cobalt in H2O2 based slurry. ECS Journal of Solid State Science and Technology, 10(4), 043006. https://doi.org/10.1149/2162-8777/abf49c
   Web of Science ®Google Scholar
• Yin, B. T., Yan, C. Y., Peng, X. M., Zhang, S. L., Rasheed, S., Geng, R. X., & Zhou, C. H. (2014). Synthesis and biological evaluation of α-triazolyl chalcones as a new type of potential antimicrobial agents and their interaction with calf thymus DNA and human serum albumin. European Journal of Medicinal Chemistry, 71, 148–159. https://doi.org/10.1016/j.ejmech.2013.11.003
   PubMed Web of Science ®Google Scholar
• Yu, X., Yang, Y., Shiyu, L., Yao, Q., Heting, L., Xiaofang, L., & Pinggui, Y. (2011). The fluorescence spectroscopic study on the interaction between imidazo [2, 1-b] thiazole analogues and bovine serum albumin. Spectrochimica Acta Part A, Molecular and Biomolecular Spectroscopy, 83(1), 322–328. https://doi.org/10.1016/j.saa.2011.08.038
   PubMed Web of Science ®Google Scholar
• Zhang, E. L., Fu, S., Wang, R. X., Li, H. X., Liu, Y., Ma, Z. Q., Liu, G. K., Zhu, C. S., Qin, G. W., & Chen, D. F. (2019). Role of Cu element in biomedical metal alloy design. Rare Metals, 38(6), 476–494. https://doi.org/10.1007/s12598-019-01245-y
   Web of Science ®Google Scholar
• Żurowska, B. (2014). Structural and magnetic characterization of Cu-picolinate and Cu-quinaldinate and their mixed complexes with water or halides. Inorganica Chimica Acta, 418, 136–152. https://doi.org/10.1016/j.ica.2014.04.007
   Web of Science ®Google Scholar