Spectral and molecular docking studies on the interaction of three flavonoids with bovine serum albumin

References

• Anusuya, S., & Gromiha, M. M. (2019). Structural basis of flavonoids as dengue polymerase inhibitors: Insight from QSAR and docking studies. Journal of Biomolecular Structure and Dynamics, 37(1), 104–115. doi:10.1080/07391102.2017.1419146
   PubMed Web of Science ®Google Scholar
• Bi, S., Song, D., Kan, Y., Xu, D., Tian, Y., Zhou, X., & Zhang, H. (2005). Spectroscopic characterization of the effective components anthraquinones in Chinese medicinal herbs binding with serum albumins. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 62(1–3), 203–212. doi:10.1016/j.saa.2004.12.049
   PubMed Web of Science ®Google Scholar
• Bi, S., Zhao, T., Wang, Y., & Zhou, H. (2016). Study on the interactions of mapenterol with serum albumins using multi-spectroscopy and molecular docking. Luminescence, 31(2), 372–379. doi:10.1002/bio.2969
   PubMed Web of Science ®Google Scholar
• Bi, S., Zhou, H., Wu, J., & Wang, Y. (2018). Interaction of dextromethorphan hydrobromide with DNA: Multispectral, voltammetric, and molecular docking technology. Journal of Biomolecular Structure and Dynamics, 36(5), 1154–1160. doi:10.1080/07391102.2017.1313781
   PubMed Web of Science ®Google Scholar
• Byler, D. M., & Susi, H. (1986). Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers, 25(3), 469–487. doi:10.1002/bip.360250307
   PubMed Web of Science ®Google Scholar
• Dewey, T. G. (1991). Fluorescence quenching reactions: Probing biological macromolecular structure. New York: Plenum Press.
   Google Scholar
• Fanali, G., Masi, A. D., Trezza, V., Marino, M., Fasano, M., & Ascenzi, P. (2012). Human serum albumin: From bench to bedside. Molecular Aspects of Medicine, 33(3), 209–290. doi:10.1016/j.mam.2011.12.002
   PubMed Web of Science ®Google Scholar
• Förster, T., & Sinanogl, O. (1966). Modern quantum chemistry (3rd ed.). London: Academic Press.
   Google Scholar
• He, X. M., & Carter, D. C. (1993). Atomic structure and chemistry of human serum albumin. Nature, 364(6435), 362–362. doi:10.1038/364362b0
   PubMed Web of Science ®Google Scholar
• Kandagal, P. B., Ashoka, S., Seetharamappa, J., Shaikh, S. M. T., Jadegoud, Y., & Ijare, O. B. (2006). Study of the interaction of an anticancer compound with human and bovine serum albumin: Spectroscopic approach. Journal of Pharmaceutical and Biomedical Analysis, 41(2), 393–399. doi:10.1016/j.jpba.2005.11.037
   PubMed Web of Science ®Google Scholar
• Lakowicz, J. R. (2006). Principles of fluorescence spectroscopy (3rd ed.). Berlin: Springer.
   Google Scholar
• Li, D., Zhu, M., Xu, C., & Ji, B. (2011). Characterization of the baicalein–bovine serum albumin complex without or with Cu2+ or Fe3+ by spectroscopic approaches. European Journal of Medicinal Chemistry, 46(2), 588–599. doi:10.1016/j.ejmech.2010.11.038
   PubMed Web of Science ®Google Scholar
• Liu, X., Ling, Z., Zhou, X., Ahmad, F., & Zhou, Y. (2016). Comprehensive spectroscopic probing the interaction and conformation impairment of bovine serum albumin (BSA) by herbicide butachlor. Journal of Photochemistry and Photobiology B: Biology, 162, 332–339. doi:10.1016/j.photobiol.2016.07.005
   PubMed Web of Science ®Google Scholar
• Mahmood, N., Pizza, C., Aquino, R., De Tommasi, N., Piacente, S., Colman, S., … Hay, A. J. (1993). Inhibition of HIV infection by flavanoids. Antiviral Research, 22(2–3), 189–199. doi:10.1016/0166-3542(93)90095-Z
   PubMed Web of Science ®Google Scholar
• Meshram, R. J., Bagul, K. T., Pawnikar, S. P., Barage, S. H., Kolte, B. S., & Gacche, R. N. (2019). Known compounds and new lessons: Structural and electronic basis of flavonoids based bioactivities. Journal of Biomolecular Structure and Dynamics, 1–29. doi:10.1080/07391102.2019.1597770
   Web of Science ®Google Scholar
• Palko-Labuz, A., Sroda-Pomianek, K., Wesolowska, O., Kostrzewa-Suslow, E., Uryga, A., & Michalak, K. (2019). MDR reversal and pro-apoptotic effects of statins and statins combined with flavonoids in colon cancer cells. Biomedicine & Pharmacotherapy, 109, 1511–1522. doi:10.1016/j.biopha.2018.10.169
   PubMed Web of Science ®Google Scholar
• Punith, R., & Seetharamappa, J. (2012). Spectral characterization of the binding and conformational changes of serum albumins upon interaction with an anticancer drug. Spectrochimica Acta A: Molecular and Biomolecular Spectroscopy, 92, 37–41. doi:10.1016/j.saa.2012.02.038
   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. doi:10.1021/bi00514a017
   PubMed Web of Science ®Google Scholar
• Shi, J. H., Lou, Y. Y., Zhou, K. L., & Pan, D. Q. (2018). Spectroscopic and molecular docking approaches for the investigation of molecular interactions between herbicide sulfosulfuron and bovine serum albumin. Journal of Biomolecular Structure and Dynamics, 36(11), 2822–2830. doi:10.1080/07391102.2017.1375991
   PubMed Web of Science ®Google Scholar
• Shi, X., Li, X., Gui, M., Zhou, H., Yang, R., Zhang, H., & Jin, Y. (2010). Studies on interaction between flavonoids and bovine serum albumin by spectral methods. Journal of Luminescence, 130(4), 637–644. doi:10.1016/j.jlumin.2009.11.008
   Web of Science ®Google Scholar
• Steiner, R. F., & Weinryb, L. (1971). Excited states of protein and nucleic acid. New York: Plenum press.
   Google Scholar
• Sudlow, G., Birkett, D. J., & Wade, D. N. (1975). The characterization of two specific compound binding sites on human serum albumin. Molecular Pharmacology, 11, 824–832.
   PubMed Web of Science ®Google Scholar
• Suganthi, G., & Elango, K. P. (2017). Binding of organophosphate insecticides with serum albumin: Multispectroscopic and molecular modelling investigations. Physics and Chemistry of Liquids, 55(2), 165–178. 1183006. doi:10.1080/00319104.2016
   Web of Science ®Google Scholar
• Sun, L., Zhang, J., & Liu, K. (2007). Electrochemical investigation of ascorbic acid interacting with bovine serum albumin. Analytical Letters, 40(16), 1775–1786. doi:10.1080/00032719908542932
   Web of Science ®Google Scholar
• Ware, W. R. (1962). Oxygen quenching of fluorescence in solution: An experimental study of the diffusion process. The Journal of Physical Chemistry, 66(3), 455–458. doi:10.1021/j100809a020
   Web of Science ®Google Scholar
• Wang, B. L., Zhou, K. L., Lou, Y. Y., Pan, D. Q., Kou, S. B., & Shi, J. H. (2019). Assessment on the binding affinity between ritonavir with model transport protein: A combined multi-spectroscopic approaches with computer simulation. Journal of Biomolecular Structure and Dynamics, 1–20. doi:10.1080/07391102.2019.1587515
   Web of Science ®Google Scholar
• Wu, D., Yan, J., Wang, J., Wang, Q., & Li, H. (2015). Characterisation of interaction between food colourant allura red AC and human serum albumin: Multispectroscopic analyses and docking simulations. Food Chemistry, 170, 423–429. doi:10.1016/j.foodchem.2014.08.088
   PubMed Web of Science ®Google Scholar
• Yuan, T., Weljie, A. M., & Vogel, H. J. (1998). Tryptophan fluorescence quenching by methionine and selenomethionine residues of calmodulin: Orientation of peptide and protein binding. Biochemistry, 37(9), 3187–3195. doi:10.1021/bi9716579
   PubMed Web of Science ®Google Scholar
• Zargari, F., Lotfi, M., Shahraki, O., Nikfarjam, Z., & Shahraki, J. (2018). Flavonoids as potent allosteric inhibitors of protein tyrosine phosphatase 1B: Molecular dynamics simulation and free energy calculation. Journal of Biomolecular Structure and Dynamics, 36(15), 4126–4142. doi:10.1080/07391102.2017.4109651
   PubMed Web of Science ®Google Scholar
• Zhang, W., Han, B., Zhao, S., Ge, F., Xiong, X., Chen, D., … Chen, C. (2010). Study on the interaction between theasinesin and bovine serum albumin by fluorescence method. Analytical Letters, 43(2), 289–299. doi:10.1018/00032710903325823
   Web of Science ®Google Scholar
• Zhou, X.-Q., Wang, B.-L., Kou, S.-B., Lin, Z.-Y., Lou, Y.-Y., Zhou, K.-L., & Shi, J.-H. (2019). Multi-Spectroscopic approaches combined with theoretical calculation to explore the intermolecular interaction of telmisartan with bovine serum albumin. Chemical Physics, 522, 285–293. doi:10.1016/j.chemphys.2019.03.019
   Web of Science ®Google Scholar