DOI QR코드

DOI QR Code

Binding Set Analysis for Interaction of Human Serum Albumin with Cethyl Trimethylammonium Bromide

  • Published : 2004.06.20

Abstract

The binding of cethyl trimethylammonium bromide, (CTAB) with human serum albumin (HSA) has been investigated at 5 mM phosphate buffer pH 7.0, 27 $^{\circ}C$ and various ionic strength using ion selective membrane electrodes. This method is faster and much more accurate than equilibrium dialysis technique, so provides sufficient and accurate data for binding data analysis. A novel and simple method was introduced for resolution and characterization of binding sets on basis of binding capacity concept. The values of Hill binding parameters were estimated for each set and used for calculation of intrinsic binding affinity. The results interpreted on basis of nature of forces which interfered in the interaction and represent the existence of three and two binding sets for binding of CTAB at $10^{-4}$ and $10^{-3}$ M of NaBr, respectively.

Keywords

References

  1. Dayhoff, M. O. Atlas of Protein Sequence and Structure; NationalBiomedical Foundation: Washington, DC, 1972.
  2. Peters, T. All about Albumin, Biochemistry, Genetics, and MedicalApplications; Academic Press: New York, 1992.
  3. Longworth, L. G.; Jacobsen, C. F. J. Phys. Colloid. Chem. 1949,53, 126. https://doi.org/10.1021/j150466a010
  4. Gianazza, E.; Firgerio, A.; Astrua-Testori, S.; Righetti, P. G.Electrophoresis 1984, 5, 310. https://doi.org/10.1002/elps.1150050512
  5. Haynes, C. A.; Norde, W. Coll. Surf., B: Biointerfaces 1994, 2,517. https://doi.org/10.1016/0927-7765(94)80066-9
  6. Peters, T. Adv. Protein Chem. 1985, 37, 161. https://doi.org/10.1016/S0065-3233(08)60065-0
  7. Soderquist, M. E.; Walton, A. G. J. Coll. Int. Sci. 1980, 75, 386. https://doi.org/10.1016/0021-9797(80)90463-4
  8. Goddard, E. D.; Ananthapadmanabhan, K. P. Interactions ofSurfactants with Polymers and Proteins; CRC Press, Inc.: Florida,1992; chapter 8.
  9. Tanford, C. The Hydrophobic Effect: Formation of Micelles and Biological Membranes, 2nd ed; Wiley-Nescience: New York,1980; chapter 14.
  10. Jones, M. N.; Brass, A. Food Polymers: Gels and Colloids;Pickinson, E., Ed.; Royal Society of Chemistry: Chambridge, 1991.
  11. Vaslescu, M.; Angelescu, D.; Almgran, M.; Valstar, A. Langmuir1999, 15, 2635. https://doi.org/10.1021/la981424y
  12. Nelson, C. A. J. Biol. Chem. 1971, 246(12), 3895.
  13. Jones, M. N. Chemical Society Reviews 1992, 21, 127. https://doi.org/10.1039/cs9922100127
  14. Gharibi, H.; Razavizadeh, B. M.; Rafati, A. A. Colloid SurfacesA: Physicochemical and Engineering Aspects 1998, 136, 123. https://doi.org/10.1016/S0927-7757(97)00305-1
  15. Jones, M. N. Biological Thermodynamics; Jones, M. N., Ed.;Elsevier: Amsterdam, 1988; p 182.
  16. Bordbar, A. K.; Saboury, A. A.; Housaindokht, M. R.; Moosavi-Movahedi, A. A. J. Coll. Int. Sci. 1997, 192, 415. https://doi.org/10.1006/jcis.1997.4999
  17. Scatchard, G. Ann. New York Acad. Sci. 1949, 51, 660. https://doi.org/10.1111/j.1749-6632.1949.tb27297.x
  18. Cera, E.; Gill, S.; Wyman, J. Proc. Natl. Acad. Sci. USA 1988, 85,449. https://doi.org/10.1073/pnas.85.2.449
  19. Dolman, D.; Gill, S. J. Anal. Biochem. 1978, 87, 127. https://doi.org/10.1016/0003-2697(78)90576-6
  20. Hill, A. V. J. Physiol. 1910, 40, 4.
  21. Tanford, C. Physical Chemistry of Macromolecules; Wiley: NewYork, 1961; chapter 9.
  22. Moosavi-Movahedi, A. A.; Housaindokht, M. R. Int. J. Biol.Macromol. 1991, 13, 50. https://doi.org/10.1016/0141-8130(91)90010-R
  23. Housaindokht, M. R.; Chamani, J.; Saboury, A. A.; Moosavi-Movahedi, A. A.; Bahrololoom, M. Bull. Korean Chem. Soc.2001, 22, 145.
  24. Bordbar, A. K.; Saboury, A. A.; Moosavi-Movahedi, A. A.Biochem. Edu. 1996, 24, 172. https://doi.org/10.1016/0307-4412(95)00122-0
  25. Bordbar, A. K.; Moosavi-Movahedi, A. A.; Amini, M. K.Thermochim. Acta 2003, 400, 95. https://doi.org/10.1016/S0040-6031(02)00483-5

Cited by

  1. Surfactantion-selective electrodes: A promising approach to the study of the aggregation of ionic surfactants in solution vol.8, pp.4, 2012, https://doi.org/10.1039/C1SM05834G
  2. Investigation of the Effects of Various Cyclodextrins on the Stabilisation of Human Serum Albumin by a Spectroscopic Method vol.68, pp.12, 2015, https://doi.org/10.1071/CH15079
  3. Bio thermodynamic studies of diclofenac interaction with lysozyme under various conditions using diclofenac-selective membrane electrode and molecular docking vol.35, pp.13, 2017, https://doi.org/10.1080/07391102.2016.1231083
  4. Computational and experimental study on the interaction of three novel rare earth complexes containing 2,9-dimethyl-1,10-phenanthroline with human serum albumin vol.15, pp.7, 2018, https://doi.org/10.1007/s13738-018-1356-5
  5. Synthesis, characterization, and binding assessment with human serum albumin of three bipyridine lanthanide(III) complexes pp.1538-0254, 2018, https://doi.org/10.1080/07391102.2018.1464959
  6. A Thermodynamic Study on the Binding of Human Serum Albumin with New Synthesized Anti Cancer Pd (II) Complex vol.37, pp.12, 2008, https://doi.org/10.1007/s10953-008-9322-y
  7. A High Performance Theory for Thermodynamic Study on the Binding of Human Serum Albumin with Erbium Chloride vol.27, pp.2, 2009, https://doi.org/10.1002/cjoc.200990046
  8. Binding and fluorescence study on interaction of human serum albumin (HSA) with cetylpyridinium chloride (CPC) vol.55, pp.1, 2007, https://doi.org/10.1016/j.colsurfb.2006.11.012
  9. Interaction of alkylpyridinium chlorides with human serum albumin studied by fluorescence techniques vol.195, pp.2, 2004, https://doi.org/10.1016/j.jphotochem.2007.10.015
  10. Conformational changes and sequence analysis in cellulase from Aspergillus niger with cationic surfactant vol.17, pp.6, 2010, https://doi.org/10.1007/s10570-010-9458-y
  11. Biological interaction of thiamine with lysozyme using binding capacity concept and molecular docking vol.34, pp.10, 2004, https://doi.org/10.1080/07391102.2015.1109553
  12. Sequestration of Cetyltrimethylammonium Bromide on Gold Nanorods by Human Serum Albumin Causes Its Conformation Change vol.36, pp.1, 2004, https://doi.org/10.1021/acs.langmuir.9b03187