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Research Articles

Spectroscopic and molecular docking studies on interaction of two Schiff base complexes with bovine serum albumin

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Pages 2650-2658 | Received 05 Dec 2018, Accepted 26 Jun 2019, Published online: 15 Jul 2019

References

  • Albani, J. R. (2007). Principles and applications of fluorescence spectroscopy, 1st ed.; Blackwell Publishing
  • Alghool, S., Zoromba, M. S., & Abd El-Halim, H. F. (2013). Lanthanide amino acid Schiff basecomplexes: Synthesis, spectroscopic characterization, physical properties and in vitro antimicrobial studies. Journal of Rare Earths, 31(7), 715–721. doi:10.1016/S1002-0721(12)60347-0
  • Amiri, M., Ajloo, D., Fazli, M., Mokhtarieh, A., Grivani, G., & Saboury, A. A. (2018). Spectroscopic, electrochemical, docking and molecular dynamics studies on the interaction of three oxovanadium (IV) Schiff base complexes with bovine serum albumin and their cytotoxicity against cancer. Journal of Biomolecular Structure and Dynamics, 36(14), 3753–3772. doi:10.1080/07391102.2017.1400467
  • Bardajee, G. R., Hooshyar, Z., Shafagh, P., Ghiasvand, S., & Kakavand, N. (2014). Combined spectroscopic and molecular docking techniques to study interaction of Zn(II) DiAmsar with serum albumins. Journal of Luminescense., 156, 55–62. doi:10.1016/j.jlumin.2014.06.042
  • Barone, G., Terenzi, A., Lauria, A., Almerico, A. M., Leal, J. M., Busto, N., & García, B. (2013). DNA-binding of nickel(II), copper(II) and zinc(II) complexes: Structure–affinity relationships. Coordination Chemistry Reviews, 257(19-20), 2848–2862. doi:10.1016/j.ccr.2013.02.023
  • Benarous, N., Cherouana, A., Aubert, E., Durand, P., & Dahaoui, S. (2016). Synthesis, characterization, crystal structure and DFT study of two new polymorphs of a Schiff base (E)-2-((2,6-dichlorobenzylidene)amino)benzonitrile. Journal of Molecular Structure, 1105, 186–193. doi:10.1016/j.molstruc.2015.10.037
  • Bourassa, P., Kanakis, C. D., Tarantilis, P., Pollissiou, M. G., & Tajmir-Riahi, H. A. (2010). Resveratrol, genistein, and curcumin bind bovine serum albumin. The Journal of Physical Chemistry B, 114(9), 348–354. doi:10.1021/jp9115996
  • Beechem, J. M., & Brand, L. (1985). Time-resolved fluorescence of proteins. Annual Review of Biochemistry, 54(1), 43–71. doi:10.1146/annurev.bi.54.070185.000355
  • Bourassa, P., & Tajmir-Riahi, H. A. (2012). Locating the Binding Sites of Folic Acid with Milk α- and β-Caseins. The Journal of Physical Chemistry B, 116(1), 513–519. doi:10.1021/jp2083677
  • Calvin, M., & Wilson, K. W. (1945). Stability of chelate compounds. Journal of the American Chemical Society, 67(11), 2003–2007. doi:10.1021/ja01227a043
  • da Silva, C. M., da Silva, D. L., Modolo, L. V., Alves, R. B., de Resende, M. A., Martins, C. V. B., & de Fátima, Â. Â. (2011). Schiff bases: A short review of their antimicrobial activities. Journal of Advanced Research, 2(1), 1–8. doi:10.1016/j.jare.2010.05.004
  • Dehkhodaei, M., Sahihi, M., & Amiri Rudbari, H. (2018). Spectroscopic and molecular docking studies on the interaction of Pd(II) & Co(II) Schiff base complexes with β-lactoglobulin as a carrier protein. Journal of Biomolecular Structure and Dynamics, 36(12), 3130–3136. doi:10.1080/07391102.2017.1380537
  • Kong, D., Qin, C., Fan, P., Li, B., & Wang, J. (2015). Spectroscopic studies on interaction of BSA and Eu(III) complexes with H5ph-dtpa and H5dtpa ligands. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 140, 372–381. doi:10.1016/j.saa.2015.01.004
  • Fasman, D. G. (1992). Practical handbook of biochemistry and molecular biology. Boston, MA: CRC Press
  • Kandagal, P. B., Ashoka, S., Seetharamappa, J., Shaikh, S. M. T., Jadegoud, Y., & Ijare, O. B. (2006). Study of the interaction of an anticancer drug with human and bovine serumalbumin: Spectroscopic approach. Journal of Pharmaceutical and Biomedical Analysis, 41(2), 393–399. doi:10.1016/j.jpba.2005.11.037
  • Kumari, S., & Chauhan, G. S. (2014). New cellulose-lysine Schiff-base-based sensor-adsorbent for mercury ions. ACS Applied Materials & Interfaces, 6(8), 5908–5917. doi:10.1021/am500820n
  • Kumar, C. V., & Tolosa, L. M. (1993). Interaction of hydrophobic probes with serum albumin-influence of the side chain and exciplex formation at the binding site. Journal of Physical Chemistry, 97(51), 13914. 19
  • Li, L., Li, Z., Wang, K., Zhao, S., Feng, J., Li, J., … Wang, Q. (2014). Design, synthesis, and biological activities of aromatic gossypol Schiff base derivatives. Journal of Agricultural and Food Chemistry, 62(46), 11080–11088. doi:10.1021/jf504411g
  • Lakowicz, J. (2013). Principles of fluorescence spectroscopy (3rd ed.). New York, NY: Kluwer Academic.
  • Licini, G., Conte, V., Coletti, A., Mba, M., & Zonta, C. (2011). Recent advances in vanadium catalyzed oxygen transfer reactions. Coordination Chemistry Reviews, 255(19/20), 2345–2357. doi:10.1016/j.ccr.2011.05.004
  • Lakshmipraba, J., & Arunachalam, S. (2010). Studies on the interactions of polymer-anchored copper(II) complexes with tRNA. Transition Metal Chemistry, 35(4), 477–482. doi:10.1007/s11243-010-9352-3
  • Liu, E. H., Qi, L. W., & Li, P. (2010). Structural relationship and binding mechanisms of five flavonoids with bovine serum albumin. Molecules (Basel, Switzerland), 15(12), 9092–9103. doi:10.3390/molecules15129092
  • Marcus, Y., & Eliezer, I. (1969). The stability of mixed complexes in solution. Coordination Chemistry Reviews, 4(3), 273–322. doi:10.1016/S0010-8545(00)80208-8
  • Molaee, H., Sahihi, M., Moghadam, M., Mirkhani, V., Shahram Tangestaninejad, S., Iraj Mohammadpoor-Baltork, I., & Amiri Rudbari, H. (2019). A combined computational/experimental study on HSA binding of two water-soluble Schiff base ligands derived from pyridine derivative and ethylendiamine. Journal of Biomolecular Structure and Dynamics, 37(3), 641–648. doi:10.1080/07391102.2018.1436091
  • Moradi-Shoeili, Z., Amini, Z., Boghaei, D. M., & Notash, B. (2013). Synthesis, X-ray structure and ascorbic oxidation properties of ternary a-amino acid Schiff base-bipy Cu(II) complexes as functional models for ascorbic oxidase. Polyhedron, 53, 76–82. doi:10.1016/j.poly.2013.01.020
  • Schmidt, U., & Prantz, E. (1977). Activation of double bonds in dehydro amino acids: A model for pyridoxal-containing enzymes in elimination-addition reactions. Angewandte Chemie International Edition in English, 16(5), 328. doi:10.1002/anie.197703281
  • Shahraki, S. F., Shiri, F., & Saeidifar, M. (2018). Synthesis, characterization, in silico ADMET prediction, and protein binding analysis of a novel zinc(II) Schiff-base complex: Application of multi-spectroscopic and computational techniques. Journal of Biomolecular Structure and Dynamics, 36(7), 1666–1680. doi:10.1080/07391102.2017.1334595
  • Shi, J. H., Pan, D. Q., Wang, X. X., Liu, T. T., Jiang, M., & Wang, Q. (2016). Characterizing the binding interaction between antimalarial artemether (AMT) and bovine serum albumin (BSA): Spectroscopic and molecular docking methods. Journal of Photochemistry and Photobiology B: Biology, 162, 14–23. doi:10.1016/j.jphotobiol.2016.06.025
  • Sigel, A., & Sigel, H. (1996). Metal ions in biological systems, interaction of metal ions with nucleotides, nucleic acids, and their constituents (Vol. 32). New York, NY: Marcel Dekker.
  • Temel, E., Alaşalvar, C., Eserci, H., & Ağar, E. (2017). Experimental (X-ray, IR and UV–vis.) and DFT studies on cocrystallization of two tautomers of a novel Schiff base compound. Journal of Molecular Structure, 1128, 5–12. doi:10.1016/j.molstruc.2016.08.038
  • Tao, T., Xu, F., Chen, X.-C., Liu, Q.-Q., Huang, W., & You, X.-Z. (2012). Comparisons between azo dyes and Schiff bases having the same benzothiazole/phenol skeleton: Syntheses, crystal structures and spectroscopic properties. Dyes and Pigments, 92(3), 916–922. doi:10.1016/j.dyepig.2011.09.008
  • Wang, G., & Chang, J. C. (1994). Copper(II) and Zinc(II) (1994) complexes of Schiff bases derived from amino acids and O-Vanillin. Synthesis and Reactivity in Inorganic and Metal-Organic Chemistry, 24(4), 623–630. doi:10.1080/00945719408000138
  • Zhang, X. P., Hou, Y. H., Wang, L., Zhang, YZh., & Liu, Y. (2013). Exploring the mechanism of interaction between sulindac and human serum albumin: Spectroscopic and molecular modeling methods. Journal of Luminescense., 138, 8–14. doi:10.1016/j.jlumin.2012.12.059

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