Multi-spectroscopic and molecular modelling approach to investigate the interaction of riboflavin with human serum albumin

References

• Ahmad, E., Rabbani, G., Zaidi, N., Singh, S., Rehan, M., Khan, M. M., … Subbarao, N. (2011). Stereo-selectivity of human serum albumin to enantiomeric and isoelectronic pollutants dissected by spectroscopy, calorimetry and bioinformatics. PLoS ONE, 6, e26186.10.1371/journal.pone.0026186
   PubMed Web of Science ®Google Scholar
• Ashoori, M., & Saedisomeolia, A. (2014). Riboflavin (vitamin B2) and oxidative stress: A review. British Journal of Nutrition, 111, 1985–1991.10.1017/S0007114514000178
   PubMed Web of Science ®Google Scholar
• Beck, M. Y., & Nagypal, I. (1990). Chemistry of complex equilibria (pp. 112–121). New York, NY: Wiley.
   Google Scholar
• Bhogale, A., Patel, N., Sarpotdar, P., Mariam, J., Dongre, P. M., Miotello, A., & Kothari, D. C. (2013). Systematic investigation on the interaction of bovine serum albumin with ZnO nanoparticles using fluorescence spectroscopy. Colloids and Surfaces B: Biointerfaces, 102, 257–264.10.1016/j.colsurfb.2012.08.023
   PubMed Web of Science ®Google Scholar
• Bolattin, M. B., Nandibewoor, S. T., Joshi, S. D., Dixit, S. R., & Chimatadar, S. A. (2016). Interaction of hydralazine with human serum albumin and effect of β-cyclodextrin on binding: Insights from spectroscopic and molecular docking techniques. Industrial & Engineering Chemistry Research, 55, 5454–5464.10.1021/acs.iecr.6b00517
   Web of Science ®Google Scholar
• Chaturvedi, S. K., Ahmad, E., Khan, J. M., Alam, P., Ishtikhar, M., & Khan, R. H. (2015). Elucidating the interaction of limonene with bovine serum albumin: A multi-technique approach. Molecular BioSystems, 11, 307–316.10.1039/C4MB00548A
   PubMed Web of Science ®Google Scholar
• Chen, G. Z., Huang, X. Z., Xu, J. G., Wang, Z. B., & Zheng, Z. Z. (1990). Method of fluorescent analysis (pp. 2–122, 2nd ed.). Beijing: Science Press.
   Google Scholar
• Chi, Z., Liu, R., Teng, Y., Fang, X., & Gao, C. (2010). Binding of oxytetracycline to bovine serum albumin: Spectroscopic and molecular modeling investigations. Journal of Agricultural and Food Chemistry, 58, 10262–10269.10.1021/jf101417w
   PubMed Web of Science ®Google Scholar
• Colombo, B., Saraceno, L., & Comi, G. (2014). Riboflavin and migraine: The bridge over troubled mitochondria. Neurological Sciences, 35, 141–144.10.1007/s10072-014-1755-z
   PubMed Web of Science ®Google Scholar
• Cyril, L., Earl, J. K., & Sperry, W. M. (1961). Biochemists handbook (p. 83). London: E & FN Epon Led. Press.
   Google Scholar
• Diaz, M., Becker, M. I., Ioannes, A. E., & Silva, E. (1996). Development of monoclonal antibodies against a riboflavin-tryptophan photoinduced adduct: Reactivity to eye lens proteins. Photochemistry and Photobiology, 63, 762–767.10.1111/php.1996.63.issue-6
   PubMed Web of Science ®Google Scholar
• Edward, J. T. (1970). Molecular volumes and the Stokes-Einstein equation. Journal of Chemical Education, 47, 261–270.10.1021/ed047p261
   Web of Science ®Google Scholar
• Elokely, K. M., & Doerksen, R. J. (2013). Docking challenge: Protein sampling and molecular docking performance. Journal of Chemical Information and Modeling, 53, 1934–1945.10.1021/ci400040d
   PubMed Web of Science ®Google Scholar
• Förster, T., & Sinanoglu, O. (1965). Modern quantum chemistry (pp. 93–137). New York, NY: Academic.
   Google Scholar
• Gao, H., Lei, L., Liu, J., Kong, Q., Chen, X., & Hu, Z. (2004). The study on the interaction between human serum albumin and a new reagent with antitumour activity by spectrophotometric methods. Journal of Photochemistry and Photobiology A: Chemistry, 167, 213–221.10.1016/j.jphotochem.2004.05.017
   Web of Science ®Google Scholar
• Guo, X. J., Sun, X. D., & Xu, S. K. (2009). Spectroscopic investigation of the interaction between riboflavin and bovine serum albumin. Journal of Molecular Structure, 931, 55–59.10.1016/j.molstruc.2007.06.035
   Web of Science ®Google Scholar
• Il’ichev, Y. V., Perry J. L., & Simon J. D. (2002). Interaction of ochratoxin a with human serum albumin. Preferential binding of the dianion and pH effects. The Journal of Physical Chemistry B, 106, 452–459.10.1021/jp012314u
   Web of Science ®Google Scholar
• Ishtikhar, M., Khan, S., Badr, G., Osama Mohamed, A. O., & Hasan Khan, R. H. (2014). Interaction of the 5-fluorouracil analog 5-fluoro-2′-deoxyuridine with ‘N’ and ‘B’ isoforms of human serum albumin: A spectroscopic and calorimetric study. Molecular BioSystems, 10, 2954–2964.
   PubMed Web of Science ®Google Scholar
• Ito, K., Inoue, S., Yamamoto, K., & Kawanishi, S. (1993). 8-Hydroxydeoxyguanosine formation at the 5′site of 5′-GG-3′sequences in double-stranded DNA by UV radiation with riboflavin. Journal of Biological Chemistry, 268, 13221–13227.
   PubMed Web of Science ®Google Scholar
• Job, P. (1928). Formation and stability of inorganic complexes in solution. Annales de Chimie et de, 9, 113e203.
   Google Scholar
• Khan, J. M., Chaturvedi, S. K., & Khan, R. H. (2013). Elucidating the mode of action of urea on mammalian serum albumins and protective effect of sodium dodecyl sulfate. Biochemical and Biophysical Research Communications, 441, 681–688.10.1016/j.bbrc.2013.10.055
   PubMed Web of Science ®Google Scholar
• Khan, S. N., Islam, B., Yennamalli, R., Sultan, A., Subbarao, N., & Khan, A. U. (2008). Interaction of mitoxantrone with human serum albumin: Spectroscopic and molecular modeling studies. European Journal of Pharmaceutical Sciences, 35, 371–382.
   PubMed Web of Science ®Google Scholar
• Li, Y., Yao, X., Jin, J., Chen, X., Hu, Z. (2007). Interaction of rhein with human serum albumin investigation by optical spectroscopic technique and modeling studies. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1774, 51–58.
   PubMedGoogle Scholar
• Lakowicz, J. R., & Weber, G. (1973). Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules. Biochemistry, 12, 4161–4170.10.1021/bi00745a020
   PubMed Web of Science ®Google Scholar
• Lee, W. Q., Affandi, I. S., Feroz, S. R., Mohamad, S. B., & Tayyab, S. (2016). Evaluation of pendimethalin binding to human serum albumin: Insights from spectroscopic and molecular modeling approach. Journal of Biochemical and Molecular Toxicology, 31, e21839. doi:10.1002/jbt.21839
   Web of Science ®Google Scholar
• Lloyd, J. B. (1971). Synchronized excitation of fluorescence emission spectra. Nature, 231, 64–65.
   Web of Science ®Google Scholar
• Miller, J. N. (1979). Recent advances in molecular luminescence analysis. Proceedings of the Analytical Division of the Chemical Society, 16, 203–208.
   Google Scholar
• Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., & Olson, A. J. (1998). Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. Journal of Computational Chemistry, 19, 1639–1662.10.1002/(ISSN)1096-987X
   Web of Science ®Google Scholar
• Pandya, P., Agarwal, L. K., Gupta, N., & Pal, S. (2014). Molecular recognition pattern of cytotoxic alkaloid vinblastine with multiple targets. Journal of Molecular Graphics and Modelling, 54, 1–9.10.1016/j.jmgm.2014.09.001
   PubMed Web of Science ®Google Scholar
• Qais, F. A., Abdullah, K. M., Alam, M. M., Naseem, I., & Ahmad, I. (2017). Interaction of capsaicin with calf thymus DNA: A multi-spectroscopic and molecular modelling study. International Journal of Biological Macromolecules, 97, 392–402.10.1016/j.ijbiomac.2017.01.022
   PubMed Web of Science ®Google Scholar
• Qais, F. A., Alam, M. M., Naseem, I., & Ahmad, I. (2016). Understanding the mechanism of non-enzymatic glycation inhibition by cinnamic acid: An in vitro interaction and molecular modelling study. RSC Advances, 6, 65322–65337.10.1039/C6RA12321J
   Web of Science ®Google Scholar
• Rohs, R., Bloch, I., Sklenar, H., & Shakked, Z. (2005). Molecular flexibility in ab initio drug docking to DNA: Binding-site and binding-mode transitions in all-atom Monte Carlo simulations. Nucleic Acids Research, 33, 7048–7057.10.1093/nar/gki1008
   PubMed Web of Science ®Google Scholar
• Ross, P. D., & Subramanian S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20, 3096–3102. 10.1021/bi00514a017
   PubMed Web of Science ®Google Scholar
• Singh, S. S., & Mehta, J. (2006). Measurement of drug–protein binding by immobilized human serum albumin-HPLC and comparison with ultrafiltration. Journal of Chromatography B, 834, 108–116.10.1016/j.jchromb.2006.02.053
   PubMed Web of Science ®Google Scholar
• Sotarosadahiro, Y., Oya, K, Ike, H, Shimada, H, Yamaguchi, S, Hiki, Y, … Mitomi, T. (2001). Thymidine phosphorylase expression and effect of doxifluridine: A phase II study. Oncology Reports, 8, 753–758.
   PubMed Web of Science ®Google Scholar
• Tanzadehpanah, H., Asoodeh, A., Mahaki, H., Mostajabodave, Z., Chamani, J., Mojallal-Tabatabaei, Z., … Moradi, M. R. (2016). Bioactive and ACE binding properties of three synthetic peptides assessed by various spectroscopy techniques. Process Biochemistry, 51, 2067–2075.10.1016/j.procbio.2016.09.017
   Web of Science ®Google Scholar
• 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, 455–461.
   PubMed Web of Science ®Google Scholar
• Xu, L., Zhu, Y., Ma, W., Kuang, H., Liu, L., Wang, L., & Xu, C. (2011). Sensitive and specific DNA detection based on nicking endonuclease-assisted fluorescence resonance energy transfer amplification. The Journal of Physical Chemistry C, 115, 16315–16321.10.1021/jp2036263
   Web of Science ®Google Scholar
• Yu, M., Ding, Z., Jiang, F., Ding, X., Sun, J., Chen, S., & Lv, G. (2011). Analysis of binding interaction between pegylated puerarin and bovine serum albumin by spectroscopic methods and dynamic light scattering. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 83, 453–460.10.1016/j.saa.2011.08.065
   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, 3187–3195.10.1021/bi9716579
   PubMed Web of Science ®Google Scholar
• Zhang, W., Zhang, Q., Wang, F., Yuan, L., Xu, Z., Jiang, F., & Liu, Y. (2015). Comparison of interactions between human serum albumin and silver nanoparticles of different sizes using spectroscopic methods. Luminescence, 30, 397–404.
   PubMed Web of Science ®Google Scholar
• Zhang, Y. Z., Zhou, B., Liu, Y. X., Zhou, C. X., Ding, X. L., & Liu, Y. (2008). Fluorescence study on the interaction of bovine serum albumin with p-aminoazobenzene. Journal of Fluorescence, 18, 109–118.10.1007/s10895-007-0247-4
   PubMed Web of Science ®Google Scholar
• Zhu, X., Wentworth, P., Kyle, R. A., Lerner, R. A., & Wilson, I. A. (2006). Cofactor-containing antibodies: Crystal structure of the original yellow antibody. Proceedings of the National Academy of Sciences of the United States of America, 103, 3581–3585.10.1073/pnas.0600251103
   PubMed Web of Science ®Google Scholar