98
Views
3
CrossRef citations to date
0
Altmetric
Letters to the Editor

Effect of monovalent ions on the thermal stability of bovine serum albumin in dimethylsulfoxide aqueous solutions. Spectroscopic approach

, &
Pages 2284-2288 | Received 13 Feb 2020, Accepted 06 Mar 2020, Published online: 31 Mar 2020

References:

  • Ahmed, M. H., Byrne, J. A., McLaughlin, J., & Ahmed, W. (2013). Study of human serum albumin adsorption and conformational change on DLC and silicon doped DLC using XPS and FTIR spectroscopy. Journal of Biomaterials and Nanobiotechnology, 4, 194–203. doi: 10.4236/jbnb.2013.42024.
  • Bandekar, J. (1992). Amide modes and protein conformation. Biochimica et Biophysica Acta1120, 123–143. doi:10.1016/0167-4838(92)90261-b
  • Bennion, B. J., & Daggett, V. (2003). The molecular basis for the chemical denaturation of proteins by urea. Proceedings of the National Academy of Sciences of the United States of America, 100, 5142–5147. doi:10.1073/pnas.0930122100
  • Borzova, V. A.,  Markossian, K. A.,  Chebotareva, N. A., Kleymenov, S .Y., Poliansky, N. B., Muranov, K. O., Stein-Margolina, V. A., Shubin, V.V., Markov, D. I., & Kurganov, B. I. (2019). Kinetics of thermal denaturation and aggregation of bovine serum albumin. PLOS ONE, 11:e0153495. doi:10.1371/journal.pone.0153495
  • Camilloni, C., Guerini Rocco, A., Eberini, I., Gianazza, E., Broglia, R. A., & Tiana G. (2008). Urea and guanidinium chloride denature protein l in different ways in molecular dynamics simulations. Biophysical Journal, 94, 4654–4661. doi:10.1529/biophysj.107.125799
  • Chang, R. (2005). Physical chemistry for the biosciences. USA: University Science Books.
  • Grigoryan, K. R., Markaryan, S. A., & Aznauryan, M. G. (2009). Effect of dimethyl sulfoxide and diethyl sulfoxide on thermal denaturation of human serum albumin. Theoretical and Experimental Cryobiology, 19, 3–9.
  • Grigoryan, K. R., & Shilajyan, A. A. (2009). Role of hydrophobic interactions at the thermal denaturation of human serum albumin and bovine serum albumin at the presence of dialkylsulfoxides. Proceedings of the YSU, 3, 3–6.
  • Grigoryan, K. R., & Shiladzhyan, A. A. (2009). The effect of solvated ions on the thermal denaturation of human serum albumin in water–dimethylsulfoxide solutions. Russian Journal of Bioorganic Chemistry, 35, 646–649. doi:10.1134/S1068162009050070.
  • Lorenz-Fonfria, V. A., & Padros, E. (2004). Curve-fitting of Fourier manipulated spectra comprising apodization, smoothing, derivation and deconvolution. Spectrochimica Acta Part A, 60, 2703–2710. doi:10.1016/j.saa.2004.01.008.
  • Loring, J. S., & Fawcett, W. (1999). Ion − solvent interactions in acetonitrile solutions of lithium, sodium, and tetraethyl ammonium perchlorate using attenuated total reflectance FTIR spectroscopy. The Journal of Physical Chemistry A, 103, 3608–3617. 10.1021/jp984606+.
  • Michelis, R., Sela, S., Zeitun, T., Geron, R., & Kristal, B. (2016). Unexpected normal colloid osmotic pressure in clinical states with low serum albumin. PLOS ONE, 11:e0159839. doi:10.1371/journal.pone.0159839
  • Michnik, A. (2003). Thermal stability of bovine serum albumin DSC study. Journal of Thermal Analysis and Calorimetry, 71, 509–519. doi:10.1023/A:1022851809481
  • Murayama, K., & Tomida, M. (2004). Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier transform infrared spectroscopy. Biochemistry, 43, 11526–11532. doi:10.1021/bi0489154
  • Nikolaidis, A., & Moschakis, T. (2017). Studying the denaturation of bovine serum albumin by a novel approach of difference – UV analysis. Food Chemistry, 215, 235–244. doi:10.1016/j.foodchem.2016.07.133
  • Sunday Nnyigide, O., & Hyun, K. (2020). Molecular dynamics studies of the protective and destructive effects of sodium dodecyl sulfate in thermal denaturation of hen egg-white lysozyme and bovine serum albumin. Journal of Biomolecular Structure and Dynamics. doi:10.1080/07391102.2020.1726209.
  • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., & Gray, T. (1995). How to measure and predict the molar absorption coefficient of a protein.  Protein Science, 4, 2411–2423. doi:10.1002/pro.5560041120
  • Peters, T. (1996). All about albumin biochemistry. Genetics and medical applications. San Diego. CA: Academic Press.
  • Poklar, N., & Vesnaver, G. (2000). Thermal denaturation of proteins studied by UV spectroscopy. Journal of Chemical Education, 77, 380–382. doi:10.1021/ed077p380
  • Routledge, K. E., Tartaglia, G. G., Platt, G. W., Vendruscolo, M., & Radford, S. E. (2009). Competition between intramolecular and intermolecular interactions in an amyloid-forming protein. Journal of Molecular Biology, 389, 776–786. doi:10.1016/j.jmb.2009.04.042
  • Khatun, S., & Riyazuddeen, (2017). Interaction of colchicine with BSA: Spectroscopic, calorimetric and molecular modeling approaches. Journal of Biomolecular Structure and Dynamics, 36, 3122–3129. doi:10.1080/07391102.2017.1384397
  • Usoltsev, D., Sitnikova, V., Kajava, A., & Uspenskaya, M. (2019). Systematic FTIR spectroscopy study of the secondary structure changes in human serum albumin under various denaturation conditions. Biomoleclus 9(8), 359–376. doi:10.3390/biom9080359
  • Van der Vusse, G. J. (2009). Albumin as fatty acid transporter. Drug Metabolism and Pharmacokinetics, 24, 300–307. doi:10.2133/dmpk.24.300
  • Vardevanyan, P. O., Antonyan, A. P., Parsadanyan, M. A., Torosyan, M. A., & Karapetian, A. T. (2016). Joint interaction of ethidium bromide and methylene blue with DNA. The effect of ionic strength on binding thermodynamic parameters. Journal of Biomolecular Structure and Dynamics, 34(7), 1377–1382. doi:10.1080/07391102.2015.1079557
  • Vardevanyan, P. O., Antonyan, A. P., Parsadanyan, M. A., & Shahinyan, M. A. (2019). Study of the influence of the ionic strength on complex-formation of ethidium bromide with poly(rA)-poly(rU). Journal of Biomolecular Structure and Dynamics, 1–6. doi:10.1080/07391102.2019.1630006
  • Yang, F., Zhang, Y., & Liang, H. (2014). Interactive association of drugs binding to human serum albumin. International Journal of Molecular Sciences, 15, 3580–3595. doi:10.3390/ijms15033580
  • Zhou, H. X., & Pang, X. (2018). Electrostatic interactions in protein structure, folding, binding, and condensation. Chemical Reviews, 118(4), 1691–1741. chemrev. 7b00305. doi:10.1021/acs

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.