Spectroscopic studies on the comparative interaction of cationic single-chain and gemini surfactants with human serum albumin

Journal of Biochemistry

Volumn 145, Issue 1, 2009, Pages 67-77

  Gull, Nuzhat ^a   Sen, Priyankar ^a   Khan, Rizwan Hasan ^a   Kabir Ud Din, ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

Aggregation; Circular dichroism; Fluorescence spectroscopy; Gemini surfactants; Human serum albumin

Indexed keywords

CATIONIC SURFACTANT; CETRIMIDE; CHAPERONE; HUMAN SERUM ALBUMIN; HYDROCARBON; SOLUBILIZER;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; COMPARATIVE STUDY; ELECTRICITY; FLUORESCENCE SPECTROSCOPY; GENETIC ENGINEERING; HYDROPHOBICITY; MEASUREMENT; MOLECULAR INTERACTION; PROTEIN BINDING; PROTEIN CONTENT; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN RENATURATION; PROTEIN SURFACTANT INTERACTION; TURBIDITY; ULTRAVIOLET SPECTROSCOPY;

CIRCULAR DICHROISM; HUMANS; SERUM ALBUMIN; SPECTROMETRY, FLUORESCENCE; SURFACE-ACTIVE AGENTS;

EID: 58149114748     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvn141     Document Type: Article

References (74)

1. Guo, X.H., Zhao, N.M., Chen, S.H., and Teixeira, J. (1990) Small angle neutron scattering study of the structure of protein/detergent complexes. Biopolymers 29, 335-346
2. Tanford, C. (1980) The Hydrophobic Effect: Formation of Micelles and Biological Membranes, 2nd edn, Chapter 14, pp. 123, Wiley Interscience, New York
3. Anson, M.L. (1939) The denaturation of proteins by detergents and bile salts. Science 90, 256-257
4. Jones, M.N. (1975) A theoretical approach to the binding of amphiphilic molecules to globular proteins. Biochem. J. 151, 109-114
5. Gull, N., Sen, P., Kabir-ud-Din, and Khan, R.H. (2007) Effect of physiological concentration of urea on the conformation of human serum albumin. J. Biochem. 141, 261-268
6. Gull, N., Kumar, S., Ahmed, B., Khan, R.H., and Kabir-ud-Din (2006) Influence of urea additives on micellar morphology/protein conformation. Colloids Surf. B. 51, 10-15
7. Pace, C.N. (1990) Measuring and increasing protein stability. TIBECH. 8, 93-98
8. Rao, P.F. and Takagi, T. (1989) Reassessment of the viscosity behaviour of sodium dodecyl sulphate-protein polypeptide complexes. J. Biochem. 106, 365-371
9. Turro, N.J., Lei, X.G., Ananthapadmanabhan, K.P., and Aronson, M. (1995) Spectroscopic probe analysis of protein-surfactant interactions: the BSA/SDS system. Langmuir 11, 2525-2533
10. Greener, J., Contestable, B.A., and Bale, M.D. (1987) Interaction of anionic surfactants with gelatin: viscosity effects. Macromolecules 20, 2490-2498
11. Shinagawa, S., Kameyama, K., and Takagi, T. (1993) Effect of salt concentration of buffer on the binding of sodium dodecyl sulphate and on the viscosity behavior of the protein polypeptide derived from bovine serum albumin in the presence of the surfactant. Biochim. Biophys. Acta. 1161, 79-84
12. Wright, A.K., Thompson, M.R., and Miller, R.L. (1975) A Study of protein-sodium dodecyl sulphate complexes by transient electric birefringence. Biochemistry 14, 3224-3228
13. Galemo, E.L., Silva, C.H., Imasato, H., and Tabak, M. (2002) Interaction of bovine (BSA) and human (HSA) with ionic surfactants: Spectroscopy and modeling. Biochim. Biophys. Acta. 1594, 84-99
14. Sun, C., Yang, J., Wu, X., Huang, X., Wang, F., and Liuh, S. (2005) Unfolding and refolding of bovine serum albumin induced by cetylpyridinium bromide. Biophys. J. 88, 3518-3524
15. Nnanna, I.A. and Xia, J. (2001) Protein Based Surfactants; Surfactant Science Series Vol. 101, Marcel Dekker, New York
16. La Mesa, C. (2005) Polymer-surfactant and protein-surfactant interactions. J. Colloid Interface Sci. 286, 148-157
17. Crieghton, T.E. (1991) Stability of folded conformations. Curr. Opin. Struct. Biol. 1, 5-16
18. Hvidt, A. and Westh, P. (1998) Different views on the stability of protein conformations, and hydrophobic effects. J. Solution Chem. 27, 395-402
19. Helenius, A. and Simons, K. (1975) Solubilization of membranes by detergents. Biochim. Biophys. Acta. 415, 29-79
20. Jones, O.T., Earnest, J.P., and McNamee, M.G. (1987) Solubilizaton and reconstruction of biological membranes in Biological Membranes: A Practical Approach. (Findley, J.B.C. and Evance, W.H., eds.) pp. 139-177, IRL Press, Oxford
21. n surfactant solutions. Langmuir 19, 1009-1016
22. Kelley, D. and McClements, D.J. (2003) Interaction of bovine serum albumin with ionic surfactants in aqueous solutions. Food Hydrocolloids 17, 73-85
23. Valster, A., Brown, W., and Almgren, M. (1999) The lysozyme-sodium dodecyl sulfate system studied by dynamic and static light scattering. Langmuir 15, 2366-2374
24. Honda, C., Kamizono, H., Matsumoto, K., and Endo, K. (2004) Studies on bovine serum albumin-sodium dodecyl sulfate complexes using pyrene fluorescence probe and 5-doxylstearic acid spin probe. J. Colloid Interface Sci. 278, 310-317
25. Santos, S.F., Zenette, D., Fischer, H., and Itri, R. (2003) A systematic study of bovine serum albumin (BSA) and sodium dodecyl sulfate (SDS) interactions by surface tension and small angle X-ray scattering. J. Colloid Interface Sci. 262, 400-408
26. Wangsakan, A., Chinachoti, P., and McClements, D.J. (2004) Effect of surfactant type on surfactant maltodextrin interactions: Isothermal titration calorimetry, surface tensiometry and ultrasonic velocimetry study. Langmuir 20, 3913-3919
27. Few, A.V., Ottewill, R.H., and Parreira, H.C. (1955) The interaction between bovine plasma albumin and dodecyltrimethylammonium bromide. Biophys. Biochim. Acta. 18, 136-137
28. Nozaki, Y., Reynolds, J.A., and Tanford, C. (1974) The interaction of a cationic detergent with bovine serum albumin and other proteins. J. Biol. Chem. 249, 4452-4459
29. Ray, S. and Chakrabarti, A. (2003) Erythroid Spectrin in miceller detergents. Cell Motil. Cytoskeleton 54, 16-28
30. McCoy, M.A. and Wyss, D.F. (2002) Structures of protein-protein complexes are docked using only NMR restraints from residual dipolar coupling and chemical shift perturbations. J. Am. Chem. Soc. 124, 2104-2105
31. Menger, F. M and Littau, C.A. (1993) Gemini Surfactants: a new class of self-assembling molecules. A. J. Am. Chem. Soc. 115, 10083-10090
32. Zana, R. and Xia, J. (2004) Gemini Surfactants (Zana, R. and Xia, J., eds.) Marcel Dekker, New York
33. Rosen, M.J. (1993) Geminis: a new generation of surfactants. Chemtech. 23, 30-33
34. Zana, R. (2002) Dimeric and oligomeric surfactants. Behavior at interface and in aqueous solution: a review. Adv. Colloid Interface Sci. 97, 205-253
35. Siddiqui, U.S., Ghosh, G., and Kabir-ud-Din (2006) Dynamic light scattering studies of additive effects on the microstructure of aqueous gemini micelles. Langmuir 22, 9874-9878
36. Kabir-ud-Din, Siddiqui, U.S., Kumar, S., and Dar, A.A. (2006) Micellization of monomeric and dimeric (Gemini) surfactants in polar non-aqueous water mixed solvent. Colloid Polym. Sci. 284, 807-812
37. Li, Y., Wang, X., and Wang, Y. (2006) Comparative studies on interactions of bovine serum albumin with cationic Gemini and single chain surfactants. J. Phys. Chem. B 110, 8499
38. Pi, Y., Shang, Y., Peng, C., Liu, H., Hu, Y., and Jiang, J. (2006) Interaction between bovine serum albumin and Gemini surfactant alkanediyl-alpha, omega-bis(dimethyldodecyl-ammonium bromide). Biopolymers 83, 243-249
39. Wu, D., Xu, G., Feng, Y., and Li, Y. (2007) Aggregation behaviors of gelatin with cationic gemini surfactant at air/water interface. Int. J. Biol. Macromol. 40, 345-50
40. Wu, D., Xu, G., Sun, Y., Zhang, H., Mao, H., and Feng, Y. (2007) Interaction between proteins and Gemini surfactant. Biomacromolecules 8, 708-712
41. He, X.M. and Carter, D.C. (1992) Atomic structure and chemistry of human serum albumin. Nature 358, 209-215
42. Peters, T., Jr. (1985) Serum albumin. Adv. Protein Chem. 37, 161-245
43. Carter, D.C. and Ho, J.X. (1994) Structure of serum albumin. Adv. Protein Chem. 45, 153-203
44. Vijai, K. K and Forster, J.F. (1967) The amphoteric behavior of bovine plasma albumin: Evidence for masked carboxylate groups in the native protein. Biochemistry 6, 1152-1159
45. Peters, T., Jr. (1996) All About Albumin Biochemistry, Genetics and Medical Applications, Academic Press, California
46. 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
47. Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J. (1951) Protein measurements with the folin phenol reagent. J. Biol. Chem. 193, 265-275
48. Chen, Y.H., Yang, J.T., and Martinez, H. (1972) Fluorescence stopped flow study of relaxation process in the binding of bilirubin to serum albumins. Biochemistry 11, 4120-4131
49. Dubin, P.L., Vea, M.E.Y., Fallon, M.A., Thé, S.S., Rigsbee, D.R., and Gan, L.M. (1990) Higher order association in polyelectrolyte-micelle complexes. Langmuir 6, 1422-1427
50. Sudbeck, E.A., Dubin, P.L., Curran, M.E., and Skelton, J. (1991) Dye solubilization in polyelectrolyte-micelle complexes. J. Colloid Interface Sci. 142, 512-517
51. Xia, J., Zhang, H., Rigsbee, D.R., Dubin, P.L., and Shaikh, T. (1993) Structural Elucidation of soluble polylectrolyte-micelle complexes: intra- Vs interpolymer association. Macromolecules 26, 2759-2766
52. Ananthapadhmanabhan, K.P. (1993) Interaction of Surfactant with Polymers and Proteins (Goddard, E.D. and Ananthapadhmanabhan, K.P., eds.) CRC Press, Boca Raton, FL
53. Corbin, J., Methlot, N., Wang, H.H., Baenziger, J.E., and Blanton, M.P. (1998) Secondary structure analysis of individual transmembrane segments of the nicotinic acetylcholine receptor by circular dichroism and fourier transform infrared spectroscopy. J. Biol. Chem. 273, 771-777
54. Birdi, K.S. (1977) Micellization, Solubilization and Microemulsion. (Mittal, K.L., ed.) p. 151, Plenum Press, New York
55. Ekwall, P., Mandell, L., and Solyom, P. (1971) The Aqueous cetyltrimethylammonium bromide solutions. J. Colloid Interface Sci. 35, 519-528
56. Imae, T., Kamiya, R., and Ikeda, S. (1985) Formation of spherical and rod-like micelles of cetyltrimethylammonium bromide in aqueous NaBr solutions. J. Colloid Interface Sci. 108, 215-225
57. Dockal, M., Carter, D.C., and Ruker, F. (2000) Conformational transitions of the three recombinant domains of human serum albumin depending on pH. J. Biol. Chem. 275, 3042-3050
58. Kelly, S.M. and Price, N.C. (1997) The application of circular dichroism to studies of protein folding and unfolding. Biochim. Biophys. Acta. 1338, 161-185
59. Price, N.C. (2000) Conformational issues in the characterization of proteins. Biotechnol. Appl. Biochem. 31, 29-40
60. Chen, Y. and Barkley, M.D. (1998) Towards understanding tryptophanyl fluorescence in proteins. Biochemistry 37, 9976-9982
61. Pace, C.N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423
62. Ghisla, S., Massey, V., Lhoste, J.M., and Mayhew, S.G. (1974) Fluorescence and optical characteristics of reduced flavines and flavoproteins. Biochemistry 13, 589-597
63. Deep, S. and Ahluwalia, J.C. (2001) Interaction of bovine serum albumin with anionic surfactants. Phys. Chem. Chem. Phys. 3, 4583-4591
64. Stryer, L. (1965) The interaction n of naphthalene dye with apohemoglobin. A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13, 482-495
65. Matulis, D. and Lovrien, R (1998) 1-Anilino-8-Naphthalene sulfonate anion-protein binding depends on ion pair formation. Biophys. J. 74, 422-429
66. Slavik, J. (1982) Anilinonaphthalene sulfonate as a probe of membrane composition and function. Biochim. Biophys. Acta. 694, 1-25
67. Daniel, E. and Weber, G. (1966) Cooperative effects in binding by bovine serum albumin. The binding of 1-Anilino-8-Naphthalene sulfonate. Fluorimetric titrations. Biochemistry 5, 1893-1900
68. Chandler, D. (2002) Hydrophobicity: two faces of water. Nature 417, 491
69. Harlt, F.U. (1996) Molecular chaperone in cellular protein folding. Nature 381, 571-580
70. Rozema, D. and Gellman, S.H. (1995) Artificial chaperones: protein refolding via sequential use of detergent and cyclodextrin. J. Am. Chem. Soc. 117, 2373-2374
71. Rozema, D. and Gellman, S.H. (1996) Artificial chaperone-assisted refolding of carbonic anhydrase B. J. Biol. Chem. 271, 3478-3487
72. Rozema, D. and Gellman, S.H. (1996) Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation. Biochemistry 35, 15760-15771
73. Nath, D. and Rao, M. (2001) Artificial chaperone mediated refolding of xylanase from an alkalophilic thermophilic bacillus sp. Eur. J. Biochem. 268, 5471-5478
74. Gloxhuber, C. and Kunstler, K. (1992) Anionic Surfactants: Biochemistry, Toxicology, Dermatology (Gloxhuber, C., ed.) Marcel Dekker, New York