Investigation on the conformational changes of bovine serum albumin in a wide pH range from 2 to 12

References

• Sun, Y.; Wu, H.; Zhao, G.; Shi, Y. Binding of amifostine to human serum albumin: A biophysical study. Luminescence 2015, 30(1), 79–85.
   PubMed Web of Science ®Google Scholar
• Gokara, M.; Malavath, T.; Kalangi, S.K.; Reddana, P.; Subramanyam. R. Unraveling the binding mechanism of Asiatic acid with human serum albumin and its biological implications. Journal of Biomolecular Structure and Dynamics 2014, 32(8), 1290–1302.
   PubMed Web of Science ®Google Scholar
• Deng, S.; Zeng, D.; Luo, Y.; Zhao, J.; Li, X.; Zhao, Z.; Zhao, T. Enhancement of cell uptake and antitumor activity of selenadiazole derivatives through interaction and delivery by serum albumin. RSC Advances 2017, 7(27), 16721–16729.
   Web of Science ®Google Scholar
• Peng, X.; Wang, X.; Qi, W.; Huang, R.; Su, R.; He, Z. Deciphering the binding patterns and conformation changes upon the bovine serum albumin-rosmarinic acid complex. Food and Function 2015, 6(8), 2712–2726.
   PubMed Web of Science ®Google Scholar
• Trnkova, L.; Bousova, I.; Kubicek, V.; Drsata, J. Binding of naturally occurring hydroxycinnamic acids to bovine serum albumin. Natural Science 2010, 2(6), 563–570.
   Google Scholar
• Singh, P.; Chowdhury, P.K. Crowding-induced quenching of intrinsic tryptophans of serum albumins: A residue-level investigation of different conformations. Journal of Physical Chemistry Letters 2013, 4(16), 2610–2617.
   Web of Science ®Google Scholar
• Saio, T.; Guan, X.; Rossi, P.; Economou, A.; Kalodimos, C.G. Structural basis for protein antiaggregation activity of the trigger factor chaperone. Science 2014, 344(6184), 1250494.
   PubMed Web of Science ®Google Scholar
• Terrell, D.; Robbins, J. Protein conformation-based disease: Getting to the heart of the matter. Annual Review of Physiology 2010, 72(72), 15–17.
   PubMed Web of Science ®Google Scholar
• Zanusso, G.; Farinazzo, A.; Fiorini, M.; Gelati, M.; Castagna, A.; Righetti, P.G.; Rizzuto, N., Monaco S. pH-dependent prion protein conformation in classical Creutzfeldt-Jakob disease. Journal of Biological Chemistry 2001, 276(44), 40377–40380.
   PubMed Web of Science ®Google Scholar
• Hu, L.; Olsen, C.; Maddux, N.; Joshi, S.B.; Volkin, D.B.; Middaugh, C.R. Investigation of protein conformational stability employing a multimodal spectrometer. Analytical Chemistry 2011, 83(24), 9399–9405.
   PubMed Web of Science ®Google Scholar
• Dollery, S.J.; Lane, K.D.; Delboy, M.G.; Roller, D.G.; Nicola, A.V. Role of the Ul45 protein in herpes simplex virus entry via Low pH-dependent endocytosis and its relationship to the conformation and function of glycoprotein B. Virus Research 2010, 149(1), 115–118.
   PubMed Web of Science ®Google Scholar
• Santra, M.K.; Panda, D. Acid-induced loss of functional properties of bacterial cell division protein FtsZ: Evidence for an alternative conformation at acidic pH. Proteins-structure Function and Bioinformatics 2007, 67(1), 177–188.
   PubMed Web of Science ®Google Scholar
• Boulet, M.; Britten, M.; Lamarche, F. Aggregation of some food proteins in aqueous dispersions: Effects of concentration, pH and ionic strength. Food Hydrocolloids 2000, 14(2), 135–144.
   Web of Science ®Google Scholar
• Liu, Y.; Guo, R. pH-dependent structures and properties of casein micelles. Biophysical Chemistry 2008, 136(2–3), 67–73.
   PubMed Web of Science ®Google Scholar
• Edri, E.; Regev, O. pH effects on BSA-dispersed carbon nanotubes studied by spectroscopy-enhanced composition evaluation techniques. Analytical Chemistry 2008, 80(11), 4049–4054.
   PubMed Web of Science ®Google Scholar
• Wishnia, A.; Pinder, T. Hydrophobic interactions in proteins: Conformation changes in bovine serum albumin below pH 5. Biochemistry 1964, 3(9), 1377–1384.
   PubMed Web of Science ®Google Scholar
• Xu, Z.Z.; Grassian, V.H. Bovine serum albumin adsorption on TiO2 nanoparticle surfaces: Effects of pH and coadsorption of phosphate on protein − surface interactions and protein structure. Journal of Physical Chemistry C 2017, 121(39), 21771–21776.
   Web of Science ®Google Scholar
• He, S.L.; Huang, M.; Ye, W.; Chen, D.C.; He, S.; Ding, L.P.; Yao, Y.J.; Wan, L.; Xu. J.Z.; Miao S.D. Conformational change of bovine serum albumin molecules at neutral pH in ultra-diluted aqueous solutions. Journal of Physical Chemistry B 2014, 118 (42), 12207–12214.
   PubMed Web of Science ®Google Scholar
• Givens, B.E.; Diklich, N.D.; Fiegel, J.; Grassian, V.H. Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle-protein interactions. Biointerphases 2017, 12(2), 02D404.
   PubMed Web of Science ®Google Scholar
• Cao, X.L.; Li, H.W.; Yue, Y.; Wu, Y. pH-induced conformational changes of BSA in fluorescent AuNCs@BSA and its effects on NCs emission. Vibrational Spectroscopy 2013, 65(3), 186–192.
   Web of Science ®Google Scholar
• Qing, H.; He, Y.L.; Sheng, F.L.; Tao, Z.Y. Effects of pH and metal ions on the conformation of bovine serum albumin in aqueous solution an attenuated total reflection (ATR) FTIR spectroscopic study. Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy 1996, 52(13), 1795–1800.
   Web of Science ®Google Scholar
• Mei, Q.X.; Lai, L.; Zhou, Z.Q.; Mei, P.; Ren, Z.H.; Zheng, Y.C.; Liu, Y. Impact of multiple quaternary ammonium salts on dynamic properties of BSA adsorption layer at different pH values. Soft Matter 2017, 13, 7273–7282.
   PubMed Web of Science ®Google Scholar
• Naveenraj, S.; Anandan, S. Binding of serum albumins with bioactive substances-nanoparticles to drugs. Journal of Photochemistry and Photobiology C Photochemistry Reviews 2013, 14(14), 53–71.
   Web of Science ®Google Scholar
• Abdel-Aziz, L.; Abdel-Fattah, L.; El-Kosasy, A.; Gaied, M. A fluorescence quenching study of the interaction of nebivolol hydrochloride with bovine and human serum albumin. Journal of Applied Spectroscopy 2015, 82(4), 620–627.
   Web of Science ®Google Scholar
• Zhang, H.M.; Zhang, C.P. Study on interaction of neodymium ions(III) with bovine serum albumin(BSA) in microemulsion condition by spectrum. Journal of Guizhou University 2004, 21(1), 64–67.
   Google Scholar
• Liu, R.; Qin, P.; Wang, L.; Zhao, X.; Liu, Y.; Hao, X. Toxic effects of ethanol on bovine serum albumin. Journal of biochemical and molecular toxicology 2010, 24(1), 66–71.
   PubMed Web of Science ®Google Scholar
• Carter, D.C.; Ho, J.X. Structure of serum albumin. Advances in Protein Chemistry 1994, 45(6), 153–203.
   PubMedGoogle Scholar
• Lakkis, J.; Villota, R. Effect of acylation on substructural properties of proteins: A study using fluorescence and circular dichroism. Journal of Agricultural and Food Chemistry 1992, 40(4), 553–560.
   Web of Science ®Google Scholar
• Wei, X.F.; Ding, X.M.; Liu, H.Z. Spectral study of the microenvironment change of aromatic amino-acid residues in BSA induced by pH. Spectroscopy and Spectral Analysis 2000, 20(4), 556–559.
   Web of Science ®Google Scholar
• Varlan, A.; Hillebrand, M. Bovine and human serum albumin interactions with 3-carboxyphenoxathiin studied by fluorescence and circular dichroism spectroscopy. Molecules 2010, 15(6), 3905–3919.
   PubMed Web of Science ®Google Scholar
• Iosin, M.; Canpean, V.; Astilean, S. Spectroscopic studies on pH-and thermally induced conformational changes of bovine serum albumin adsorbed onto gold nanoparticles. Journal of Photochemistry and Photobiology A Chemistry 2011, 217(2–3), 395–401.
   Web of Science ®Google Scholar
• Burstein, E.A.; Vedenkina, N.S.; Ivkova, M.N. Fluorescence and the location of tryptophan residues in protein molecules. Photochemistry and Photobiology 1973, 18(4), 263.
   PubMed Web of Science ®Google Scholar
• Bhogale, A.; Patel, N.; Sarpotdar, P.; Mariam, J.; Dongre, P.M.; Miotello, A.; Kothari, D.C. Systematic investigation on the interaction of bovine serum albumin with ZnO nanoparticles using fluorescence spectroscopy. Colloids and Surfaces B Biointerfaces 2013, 102(22), 257–264.
   PubMed Web of Science ®Google Scholar
• Ma, F.; Sun, C.; Zhou, W.; Xu, C.; Zhou, J.; Wang, G.; Yang, X.D. Investigation and comparison of bovine hemoglobin binding to Al13, and Al(III): Evidences from spectroscopic studies. Spectrochim. Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy 2012, 97(6), 885–891.
   PubMed Web of Science ®Google Scholar
• Yu, X.; Liu, R.; Yi, R.; Yang, F.; Huang, H.; Chen, J.; Ji, D.; Yang, Y.; Li, X.; Yi, P. Study of the interaction between N-confused porphyrin and bovine serum albumin by fluorescence spectroscopy. Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy 2011, 78(4), 1329–1335.
   PubMed Web of Science ®Google Scholar
• Chi, Z.; Zhao, J.; You, H.; Wang, M. Study on the mechanism of interaction between phthalate acid esters and bovine hemoglobin. Journal of Agricultural and Food Chemistry 2016, 64(30), 6035–6041.
   PubMed Web of Science ®Google Scholar