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Conformational Study of Human Serum Albumin in Pre-denaturation Temperatures by Differential Scanning Calorimetry, Circular Dichroism and UV Spectroscopy

  • Rezaei-Tavirani, Mostafa (Faculty of Medicine, Medical University of Ilam) ;
  • Moghaddamnia, Seyed Hassan (Faculty of Paramedical Sciences, Shahid Beheshti University of Medical Sciences and Health Services) ;
  • Ranjbar, Bijan (Department of Biophysics, Faculty of Science, Tarbiat Modarres University) ;
  • Amani, Mojtaba (Department of Biophysics, Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Marashi, Sayed-Amir (Department of Biotechnology, University College of Science, University of Tehran)
  • Received : 2006.01.07
  • Accepted : 2006.05.04
  • Published : 2006.09.30
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Abstract

Thermal conformational changes of human serum albumin (HSA) in phosphate buffer, 10 mM at pH = 7 are investigated using differential scanning calorimetric (DSC), circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature increment from $25^{\circ}C$ to $55^{\circ}C$ induces reversible conformational changes in the structure of HSA. Conformational change of HSA are shown to be a three-step process. Interestingly, melting temperature of the last domain is equal to the maximum value of fever in pathological conditions, i.e. $42^{\circ}C$. These conformational alterations are accompanied by a mild alteration of secondary structures. Study of HSA-SDS (sodium dodecyl sulphate) interaction at $45^{\circ}C$ and $35^{\circ}C$ reveals that SDS affects the HSA structure at least in three steps: the first two steps result in more stabilization and compactness of HSA structure, while the last one induces the unfolding of HSA. Since HSA has a more affinity for SDS at $45^{\circ}C$ compared to $35^{\circ}C$, It is suggested that the net negative charge of HSA is decreased in fever, which results in the decrease of HSA-associated cations and plasma osmolarity, and consequently, heat removal via the increase in urine volume.

Keywords

References

  1. Bhattacharya, A. A., Grüne, T. and Curry, S. (2000) Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. J. Mol. Biol. 303, 721-732. https://doi.org/10.1006/jmbi.2000.4158
  2. Bougie, I., Parent, A. and Bisaillon, M. (2004) Thermodynamics of ligand binding by the yeast mRNA-capping enzyme reveals different modes of binding. Biochem. J. 384, 411-420. https://doi.org/10.1042/BJ20041112
  3. Brown, J. R. (1977) Albumin structure, function and uses, Rosenoer, V. M., Oratz, M., Rothschild, M. A. (eds.), Pergamon Press, Oxford, UK.
  4. Carter, D. C. and Ho, J. X. (1994) Structure of serum albumin. Adv. Protein Chem. 45, 153-203. https://doi.org/10.1016/S0065-3233(08)60640-3
  5. Chen, Y. H., Yang, J. T. and Martinez, H. M. (1972) Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11, 4120-4131. https://doi.org/10.1021/bi00772a015
  6. Curry, S., Mandelkow, H., Brick, P. and Franks, N. (1998) Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nature Struct. Biol. 5, 827-835. https://doi.org/10.1038/1869
  7. Curry, S., Brick, P. and Franks, N. P. (1999) Fatty acid binding to human serum albumin: new insights from crystallographic studies. Biochim. Biophys. Acta 1441, 131-140. https://doi.org/10.1016/S1388-1981(99)00148-1
  8. Dill, K. A., Alonso, D. O. V. and Hutchinson, K. (1989) Thermal stabilities of globular proteins, Biochemistry 28, 5439-5449. https://doi.org/10.1021/bi00439a019
  9. Farruggia, B. and Pico, G. A. (1999) Thermodynamic features of the chemical and thermal denaturations of human serum albumin. Int. J. Biol. Macromol. 26, 317-323. https://doi.org/10.1016/S0141-8130(99)00054-9
  10. Farruggia, B., Rodriguez, F., Rigatuso, R., Fidelio, G. and Pico G. (2001) The participation of human serum albumin domains in chemical and thermal unfolding. J. Protein Chem. 20, 81-89. https://doi.org/10.1023/A:1011000317042
  11. Flora, K., Brennan, J. D., Baker, G. A., Doody, M. A and Bright, F. V. (1998) Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods. Biophys. J. 75, 1084-1096. https://doi.org/10.1016/S0006-3495(98)77598-8
  12. Galisteo, M., Mateo, P. and Sanchez-Ruiz, J. (1991) Kinetic study on the irreversible thermal denaturation of yeast phosphoglycerate kinase. Biochemistry 30, 2061-2066. https://doi.org/10.1021/bi00222a009
  13. Gelamo, E. L. and Tabak, M. (2000) Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants. Spectrochimica Acta A 56, 2255-2271. https://doi.org/10.1016/S1386-1425(00)00313-9
  14. Giancola, C., De Sena, C., Fessas, D., Graziano, G. and Barone, G. (1997) DSC studies on bovine serum albumin denaturation: Effects of ionic strength and SDS concentration. Int. J. Biol. Macromol. 20, 193-204. https://doi.org/10.1016/S0141-8130(97)01159-8
  15. He, X. M. and Carter, D. C. (1992) Atomic structure and chemistry of human serum albumin. Nature 358, 209-215. https://doi.org/10.1038/358209a0
  16. Ikeguchi, M., Sugai, S., Fujino, M., Sugawara, T. and Kuwajima K. (1992) Contribution of the 6-120 disulfide bond of $\alpha$-lactalbumin to the stabilities of its native and molten globule states. Biochemistry 31, 12695-12700.
  17. Kragh-Hansen, U. (1981) Molecular aspects of ligand binding to serum albumin. Pharmacol. Rev. 33, 17-53.
  18. Kragh-Hansen, U., Hellec, F., de Foresta, B., le Maire, M. and Moller J. V. (2001) Detergents as probes of hydrophobic binding cavities in serum albumin and other water-soluble proteins. Biophys. J. 80, 2898-2911. https://doi.org/10.1016/S0006-3495(01)76255-8
  19. Michnik, A. (2003) Thermal stability of bovine serum albumin: DSC study. J. Therm. Anal. Cal. 71, 509-519. https://doi.org/10.1023/A:1022851809481
  20. Moosavi-Movahedi, A. A., Naderi, G. A. and Farzami, B. (1994) The denaturation behaviour of calmodulin in sodium n-dodecyl sulphate, dodecyl trimethyl ammonium bromide, guanidine hydrochloride and urea. Thermochimica Acta 239, 61-71. https://doi.org/10.1016/0040-6031(94)87056-X
  21. Moosavi-Movahedi, A. A., Nazari, K. and Saboury, A. A. (1997) Denaturation of horseradish peroxidase with SDS and DTAB, Colloids Surf. B. Biointerfaces 9, 123-130. https://doi.org/10.1016/S0927-7765(97)00016-7
  22. Moosavi-Movahedi, A. A. (2005) Thermodynamics of protein denaturation by sodium dodecyl sulfate. J. Iran Chem. Soc. 2, 189-196. https://doi.org/10.1007/BF03245921
  23. Nielsen, A. D., Borch, K. and Westh, P. (2000) Thermochemistry of the specific binding of C12 surfactants to bovine serum albumin. Biochim. Biophys. Acta 1479, 321-331. https://doi.org/10.1016/S0167-4838(00)00012-1
  24. Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280. https://doi.org/10.1016/0076-6879(86)31045-0
  25. Pace, C. N. (1990) Conformational stability of globular proteins. Trends Biochem. Sci. 15, 14-17. https://doi.org/10.1016/0968-0004(90)90124-T
  26. Pico, G. A. (1997) Thermodynamic features of the thermal unfolding of human serum albumin. Int. J. Biol. Macromol. 20, 63-73. https://doi.org/10.1016/S0141-8130(96)01153-1
  27. Privalov, P. L. (1982) Stability of proteins. Proteins which do not present a single cooperative system. Adv. Protein Chem. 35, 1-104. https://doi.org/10.1016/S0065-3233(08)60468-4
  28. Privalov, P. L. (1996) Intermediate states in protein folding. J. Mol. Biol. 258, 707-725. https://doi.org/10.1006/jmbi.1996.0280
  29. Privalov, P. L. and Potekhin, S. A. (1986) Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol. 131, 4-51. https://doi.org/10.1016/0076-6879(86)31033-4
  30. Ptitsyn, O. B. (1994) Kinetic and equilibrium intermediates in protein folding. Protein Eng. 7, 593-596. https://doi.org/10.1093/protein/7.5.593
  31. Ptitsyn, O. B. (1995) Structures of folding intermediates. Curr. Opin. Struct. Biol. 5, 74-78. https://doi.org/10.1016/0959-440X(95)80011-O
  32. Redfield, C., Smith, R. A. G. and Dobson, C. M. (1994) Structural characterization of a highly-ordered 'molten globule' at low pH. Nat. Struct. Biol. 1, 23-29. https://doi.org/10.1038/nsb0194-23
  33. Rezaei-Tavirani, M., Moosavi-Movahedi, A. A., Saboury, A. A., Hakimelahi, G. H., Ranjbar, B. and Housaindokht M. R. (2002) Thermodynamic domain analysis of fresh and incubated human apotransferrin. Thermochimica Acta 383, 103-108. https://doi.org/10.1016/S0040-6031(01)00684-0
  34. Saboury, A. A., Hosseini-Kishani, F., Rezaei-Tawirani, M. and Ranjbar, B. (2003) Thermodynamic studies on the interaction of nickel with human serum albumin, Progress Biochem. Biophys. 30, 732-737.
  35. Santoro, M. and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27, 8063-8068. https://doi.org/10.1021/bi00421a014
  36. Shaklai, N., Garlick, R. L. and Bunn, H. F. (1984) Nonenzymatic glycosylation of human serum albumin alters its conformation and function. J. Biol. Chem. 259, 3812-3817.
  37. Sugio, S., Kashima, A.,. Mochizuki, S., Noda, M. and Kobayashi, K. (1999) Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 12, 439-446. https://doi.org/10.1093/protein/12.6.439
  38. Tanford, C. (1968) Protein denaturation. Adv. Protein Chem. 23, 121-282. https://doi.org/10.1016/S0065-3233(08)60401-5
  39. Wallevik, K. (1973) Reversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation. J. Biol. Chem. 248, 2650-2655.
  40. Wetlaufer, D. B. (1981) Folding of protein fragments, Adv. Protein Chem. 34, 61-92. https://doi.org/10.1016/S0065-3233(08)60518-5
  41. Wetzel, R., Becker, M., Behlke, J., Billwitz, H., Bohm, S., Ebert, B., Hamann, H., Krumbiegel, J. and Lassmann, G. (1980) Temperature behaviour of human serum albumin. Eur. J. Biochem. 104, 469-478. https://doi.org/10.1111/j.1432-1033.1980.tb04449.x
  42. Yamasaki, M., Yano, H. and Aoki, K. (1992) Differential scanning calorimetric studies on bovine serum albumin: III. Effect of sodium dodecyl sulphate. Int. J. Biol. Macromol. 14, 305-312. https://doi.org/10.1016/S0141-8130(05)80070-4

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