Multi-spectroscopic and voltammetric evidences for binding, conformational changes of bovine serum albumin with thiamine

References

• Ahalawat, N., & Murarka, R. K. (2015). Conformational changes and allosteric communications in human serum albumin due to ligand binding. Journal of Biomolecular Structure and Dynamics, 33, 2192–2204. doi:10.1080/07391102.2014.996609
   PubMed Web of Science ®Google Scholar
• Awasthi, S., & Saraswathi, N. T. (2015). Elucidating the molecular interaction of sinigrin, a potent anticancer glucosinolate from cruciferous vegetables with bovine serum albumin: Effect of methylglyoxal modification. Journal of Biomolecular Structure and Dynamics, 21, 1–9. doi:10.1080/07391102.2015.1110835
   Web of Science ®Google Scholar
• Begley, T. P., Chatterjee, A., Hanes, J. W., Hazra, A., & Ealick, S. E. (2008). Cofactor biosynthesis – Still yielding fascinating new biological chemistry. Current Opinion in Chemical Biology, 12, 118–125. doi:10.1016/j.cbpa.2008.02.006
   PubMed Web of Science ®Google Scholar
• Brauner, J. W., Flach, C. R., & Mendelsohn, R. (2005). A quantitative reconstruction of the amide I contour in the IR spectra of globular proteins: From structure to spectrum. Journal of American Chemical Society, 127, 100–109. doi:10.1021/ja0400685
   PubMed Web of Science ®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 Agriculture and Food Chemistry, 58, 10262–10269. doi:10.1021/jf101417w
   PubMed Web of Science ®Google Scholar
• Cui, F., Fan, J., Li, J., & Hu, Z. (2004). Interactions between 1-benzoyl-4-p-chlorophenyl thiosemicarbazide and serum albumin: Investigation by fluorescence spectroscopy. Bioorganic and Medicinal Chemistry, 12, 151–157. doi:10.1016/j.bmc.2003.10.018
   PubMed Web of Science ®Google Scholar
• Deepa, S., & Mishra, A. K. (2005). Fluorescence spectroscopic study of serum albumin-bromadiolone interaction: Fluorimetric determination of bromadiolone. Journal of Pharmaceutical and Biomedical Analysis, 38, 556–563. doi:10.1016/j.jpba.2005.01.023
   PubMed Web of Science ®Google Scholar
• Dufour, C., & Dangles, O. (2005). Flavonoid-serum albumin complexation: Determination of binding constants and binding sites by fluorescence spectroscopy. BBA General Subjects, 1721, 164–173. doi:10.1016/j.bbagen.2004.10.013
   PubMed Web of Science ®Google Scholar
• Förster, T., & Sinanoglu, O. (1966). Modern quantum chemistry (pp. 136–146). New York, NY: Academic Press.
   Google Scholar
• Ge, S., Kojio, K., Takahara, A., & Kajiyama, T. (1998). Bovine serum albumin adsorption onto immobilized organotrichlorosilane surface: Influence of the phase separation on protein adsorption patterns. Journal of Biomaterials Science, Polymer Edition, 9, 131–150. doi:10.1163/156856298X00479
   PubMed Web of Science ®Google Scholar
• Gokara, M., Kimavath, G. B., Podile, A. R., & Subramanyam, R. (2015). Differential interactions and structural stability of chitosan oligomers with human serum albumin and α-1-glycoprotein. Journal of Biomolecular Structure and Dynamics, 33, 196–210. doi:10.1080/07391102.2013.868321
   PubMed Web of Science ®Google Scholar
• He, W., Li, Y., Xue, C., Hu, Z., Chen, X., & Sheng, F. (2005). Effect of Chinese medicine alpinetin on the structure of human serum albumin. Bioorganic and Medicinal Chemistry, 13, 1837–1845. doi:10.1016/j.bmc.2004.11.038
   PubMed Web of Science ®Google Scholar
• Heberer, T. (2002). Occurrence, fate, and removal of pharmaceutical residues in the aquatic environment: A review of recent research data. Toxicology Letters, 131, 5–17. doi:10.1016/S0378-4274(02)00041-3
   PubMed Web of Science ®Google Scholar
• Hosseinzadeh, R., & Khorsandi, K. (2016). Interaction of vitamin B1 with bovine serum albumin investigation using vitam in B1selective electrode: Potentiometric and molecular modeling study. Journal of Biomolecular structure and dynamics, 34, 1903–1910. doi:10.1080/07391102.2015.1094414.
   PubMed Web of Science ®Google Scholar
• Hosseinzadeh, R., Khorsandi, K., Hasani, V. S., & Khatibi, A. (in press). Biological interaction of thiamine with lysozyme using binding capacity concept and molecular docking. Journal of Biomolecular structure and dynamics. doi:10.1080/07391102.2015.1109553
   Web of Science ®Google Scholar
• Hu, Y. J., Liu, Y., Zhao, R. M., Dong, J. X., & Qu, S. S. (2006). Spectroscopic studies on the interaction between methylene blue and bovine serum albumin. Journal of Photochemistry and Photobiology A: Chemistry, 179, 324–329. doi:10.1016/j.jphotochem.2005.08.037
   Web of Science ®Google Scholar
• Hu, Y. J., Yang, Y. O., Bai, A. M., Li, W., & Liu, Y. (2010). Investigation of the interaction between ofloxacin and bovine serum albumin: Spectroscopic approach. Journal of Solution Chemistry, 39, 709–717. doi:10.1007/s10953-010-9527-8
   Web of Science ®Google Scholar
• Huang, B. X., & Kim, H. (2004). Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry. American Society for Mass Spectrometry, 15, 1237–1247. doi:10.1016/j.jasms.2004.05.004
   PubMed Web of Science ®Google Scholar
• Kabir, M. Z., Feroz, S. R., Mukarram, A. K., Alias, Z., Mohamad, S. B., & Tayyab, S. (2016). Interaction of a tyrosine kinase inhibitor, vandetanib with human serum albumin as studied by fluorescence quenching and molecular docking. Journal of Biomolecular Structure and Dynamics, 34, 1693–1704. doi:10.1080/07391102.2015.1089187
   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 drug with human and bovine serum albumin: Spectroscopic approach. Journal of Pharmaceutical and Biomedical Analysis, 41, 393–399. doi:10.1016/j.jpba.2005.11.037
   PubMed Web of Science ®Google Scholar
• Karthikeyan, S., Bharanidharan, G., Kesherwani, M., Mani, K. A., Srinivasan, N., Velmurugan, D., … Ganesan, S. (2016). Insights into the binding of thiosemicarbazone derivatives with human serum albumin: Spectroscopy and molecular modelling studies. Journal of Biomolecular Structure and Dynamics, 34, 1264–1281. doi:10.1080/07391102.2015.1075905
   PubMed Web of Science ®Google Scholar
• Kathleen Mahan, L., & Escott-Stump, S. (2004). Krause’s food, nutrition, & diet therapy. Ann Arbor: The University of Michigan, Saunders.
   Google Scholar
• Lackowicz, J. R. (1999). Principles of fluorescence spectroscopy. New York, NY: Kluwer Academic/Plenum Publishers.10.1007/978-1-4757-3061-6
   Google Scholar
• Lakowicz, J. R. (2006). Principles of fluorescence spectroscopy. New York, NY: Springer Science Business Media.10.1007/978-0-387-46312-4
   Google Scholar
• Lakowicz, J. R., & Weber, G. (1973). Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry, 12, 4171–4179. doi:10.1021/bi00745a021
   PubMed Web of Science ®Google Scholar
• Lehrer, S. S. (1971). Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide Ion. Biochemistry, 10, 3254–3263. doi:10.1021/bi00793a015
   PubMed Web of Science ®Google Scholar
• Lin, S. Y., Wei, Y. S., Li, M. J., & Wang, S. L. (2004). Effect of ethanol or/and captopril on the secondary structure of human serum albumin before and after protein binding. European Journal of Pharmaceutical and Biopharmaceutics, 57, 457–464. doi:10.1016/j.ejpb.2004.02.005
   PubMed Web of Science ®Google Scholar
• Lissi, E., & Abuin, E. (2011). On the evaluation of the number of binding sites in proteins from steady state fluorescence measurements. Journal of Fluorescence, 21, 1831–1833. doi:10.1007/s10895-011-0887-2
   PubMed Web of Science ®Google Scholar
• Lu, J. Q., Jin, F., Sun, T. Q., & Zhou, X. W. (2007). Multi-spectroscopic study on interaction of bovine serum albumin with lomefloxacin-copper(II) complex. International Journal of Biological Macromolecules, 40, 299–304. doi:10.1016/j.ijbiomac.2006.08.010
   PubMed Web of Science ®Google Scholar
• Miller, J. N. (1984). Recent developments in fluorescence and chemilumniscence analysis. Analyst, 109, 191–198. doi:10.1039/AN9840900191
   Web of Science ®Google Scholar
• Mote, U. S., Bhattar, S. L., Patil, S. R., & Kolekar, G. B. (2010). Interaction between felodipine and bovine serum albumin: Fluorescence quenching study. Luminescence, 25, 1–8. doi:10.1002/bio.1130
   PubMed Web of Science ®Google Scholar
• Neelam, S., Gokara, M., Sudhamalla, B., Amooru, D. G., & Subramanyam, R. (2010). Interaction studies of coumaroyltyramine with human serum albumin and its biological importance. The Journal of Physical Chemistry B, 114, 3005–3012. doi:10.1021/jp910156k
   PubMed Web of Science ®Google Scholar
• Rahmelow, K., & Hubner, W. (1996). Secondary structure determination of proteins in aqueous solution by infrared spectroscopy: A comparison of multivariate data analysis methods. Analytical Biochemistry, 241, 5–13. doi:10.1006/abio.1996.0369
   PubMed Web of Science ®Google Scholar
• Rahnama, E., Mahmoodian-Moghaddam, M., Khorsand-Ahmadi, S., Saberi, M. R., & Chamani, J. (2015). Binding site identification of metformin to human serum albumin and glycated human serum albumin by spectroscopic and molecular modeling techniques: A comparison study. Journal of Biomolecular Structure and Dynamics, 33, 513–533. doi:10.1080/07391102.2014.893540
   PubMed Web of Science ®Google Scholar
• Rezwan, K., Meier, L. P., Rezwan, M., Voros, J., Textor, M., & Gauckler, L. J. (2004). Bovine serum albumin adsorption onto colloidal Al2O3 particles: A new model based on zeta potential and UV–vis measurements. Langmuir, 20, 10055–10061. doi:10.1021/la048459k
   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. doi:10.1021/bi00514a017
   PubMed Web of Science ®Google Scholar
• Serratos, I. N., Perez-Hernandez, G., Garza-Ramos, G., Hernandez-Arana, A., Gonzalez-Mondragon, E., & Zubillaga, R. A. (2011). Binding thermodynamics of phosphorylated inhibitors to triosephosphate isomerase and the contribution of electrostatic interactions. Journal of Molecular Biology, 405, 158–172. doi:10.1016/j.jmb.2010.10.018
   PubMed Web of Science ®Google Scholar
• Subramanyam, R., Gollapudi, A. K., Bonigala, P., Chinnaboina, M., & Amooru, D. G. (2009). Betulinic acid binding to human serum albumin: A study of protein conformation and binding affinity. Journal of Photochemistry and Photobiology B: Biology, 94, 8–12. doi:10.1016/j.jphotobiol.2008.09.002
   PubMed Web of Science ®Google Scholar
• Tian, J., Liu, J., Hu, Z., & Chen, X. (2005). Interaction of wogonin with bovine serum albumin. Bioorganic and Medicinal Chemistry, 13, 4124–4129. doi:10.1016/j.bmc.2005.02.065
   PubMed Web of Science ®Google Scholar
• Valeur, B. (2001). Molecular fluorescence: Principle and applications (pp. 69–80). New York, NY: Wiley.10.1002/3527600248
   Google Scholar
• Varlan, A., & Hillebrand, M. (2010). Bovine and human serum albumin interactions with 3-carboxyphenoxathiin studied by fluorescence and circular dichroism spectroscopy. Molecules, 15, 3905–3919. doi:10.3390/molecules15063905
   PubMed 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, 455–458. doi:10.1021/j100809a020
   Web of Science ®Google Scholar
• Webb, M. E., Marquet, A., Mendel, R. R., Rebeill, F., & Smith, A. G. (2007). Elucidating biosynthetic pathways for vitamins and cofactors. Natural Product Reports, 24, 988–1008. doi:10.1039/B703105J
   PubMed Web of Science ®Google Scholar
• Wi, S., Pancoska, P., & Keiderling, T. A. (1998). Predictions of protein secondary structures using factor analysis on fourier transform infrared spectra: Effect of fourier self-deconvolution of the amide I and amide II bands. Biospectroscopy, 4, 93–106. doi:10.1002/(SICI)1520-6343(1998)4:2<93:AID-BSPY2>3.0.CO;2-T
   PubMedGoogle Scholar
• Wyngaarden, J. B., & Smith, L. H. (1988). Cecil’s textbook of medicine (18th ed.). Philadelphia, PA: W B Saunders.
   Google Scholar
• Xiao, J., Shi, J., Cao, H., Wu, S., Ren, F., & Xu, M. (2007). Analysis of binding interaction between puerarin and bovine serum albumin by multi-spectroscopic method. Journal of Pharmaceutical and Biomedical Analysis, 45, 609–615. doi:10.1016/j.jpba.2007.08.032
   PubMed Web of Science ®Google Scholar
• Yeggoni, D. P., Rachamallu, A., Kallubai, M., & Subramanyam, R. (2015). Cytotoxicity and comparative binding mechanism of piperine with human serum albumin and α-1-acid glycoprotein. Journal of Biomolecular Structure and Dynamics, 33, 1336–1351. doi:10.1080/07391102.2014.947326
   PubMed Web of Science ®Google Scholar
• Zhang, H. X., & Mei, P. (2009). In vitro binding of furadan to bovine serum albumin. Journal Solution Chemistry, 38, 351–361. doi:10.1007/s10953-009-9371-x
   Web of Science ®Google Scholar
• Zhang, Y. Z., Zhang, N. X., Ren, A. Q., Zhang, J., Dai, J., & Liu, Y. (2010). Spectroscopic studies on the interaction of 2,4-dichlorophenol with bovine serum albumin. Journal of Solution Chemistry, 39, 495–510. doi:10.1007/s10953-010-9518-9
   Web of Science ®Google Scholar
• Zhu, J., Zhang, X., Li, D., & Jin, J. (2007). Probing the binding of flavonoids to catalase by molecular spectroscopy. Journal of Molecular Structure, 843, 38–44. doi:10.1016/j.molstruc.2006.12.033
   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, 6–14. doi:10.1186/1472-6807-3-6
   PubMedGoogle Scholar