Photocontrol of protein folding: The interaction of photosensitive surfactants with bovine serum albumin

Biochemistry

Volumn 44, Issue 2, 2005, Pages 524-536

  Lee Jr , C Ted ^a,b   Smith, Kenneth A ^a   Hatton, T Alan ^a  

^a Massachusetts Institute of Technology   (United States)

^b University of Southern California   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BENZENE; HYDROPHOBICITY; INFORMATION ANALYSIS; IRRADIATION; ISOMERIZATION; LIGHT SCATTERING; NEUTRON SCATTERING; PH EFFECTS; PHOTOSENSITIVITY; ULTRAVIOLET RADIATION; X RAY CRYSTALLOGRAPHY;

BOVINE SERUM ALBUMIN (BSA); PROTEIN ELONGATION; PROTEIN FOLDING; SMALL-ANGLE NEUTRON-SCATTERING (SANS);

PROTEINS;

AZOBENZENE; SERUM ALBUMIN; SURFACTANT;

ARTICLE; CARBOXY TERMINAL SEQUENCE; ISOMERIZATION; LIGHT; LIGHT IRRADIANCE; MOLECULAR MODEL; NEUTRON SCATTERING; PH; PHOTOREACTIVITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; ULTRAVIOLET RADIATION; X RAY CRYSTALLOGRAPHY;

AZO COMPOUNDS; FLUORESCENT DYES; LIGHT; MODELS, CHEMICAL; NEUTRONS; OXAZINES; PHOTOCHEMISTRY; PHOTOSENSITIZING AGENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; QUATERNARY AMMONIUM COMPOUNDS; SCATTERING, RADIATION; SERUM ALBUMIN, BOVINE; SURFACE-ACTIVE AGENTS; ULTRAVIOLET RAYS;

BOVINAE;

EID: 12144249590     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048556c     Document Type: Article

References (81)

1. Creighton, T. E. (1993) Proteins: Structure and Molecular Properties, 2nd ed., W. H. Freeman, New York.
2. Ibel, K., May, R. P., Kirschner, K., Szadkowski, H., Mascher, E., and Lundahl, P. (1990) Protein-decorated micelle structure of sodium-dodecyl- sulfate-protein complexes as determined by neutron scattering, Eur. J. Biochem. 190, 311-318.
3. Anantbapadmanabhan, K. P. (1993) in Interaction of Surfactants with Polymers and Proteins (Goddard, E. D., and Ananthapadmanabhan, K. P., Eds.) pp 319-365, CRC Press. Boca Raton, FL.
4. 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.
5. Shirahama, K., Tsujii, K., and Takagi, T. (1974) Free-boundary electrophoresis of sodium dodecyl sulfate (SDS)-protein polypeptide complexes with special reference to SDS-polyacrylamide gel electrophoresis, J. Biochem. 75, 309-319.
6. Tanford, C. (1980) The Hydrophobic Effect: Formation of Micelles and Biological Membranes, 2nd ed., Wiley, New York.
7. Reynolds, J. A., and Tanford, C. (1970) Gross conformation of protein-sodium dodecyl sulfate complexes, J. Biol. Chem. 245, 5161-5165.
8. Lundahl, P., Greijer, E., Sandberg, M., Cardell, S., and Eriksson, K. O. (1986) A model for ionic and hydrophobic interactions and hydrogen-bonding in sodium dodecyl sulfate-protein complexes, Biochim. Biophys. Acta 873, 20-26.
9. Tanner, R. E., Herpigny, B., Chen, S. H., and Rha, C. K. (1982) Conformational change of protein sodium dodecyl sulfate complexes in solution: A study of dynamic light scattering, J. Chem. Phys. 76, 3866-3872.
10. Chen, S. H., and Teixeira, J. (1986) Structure and fractal dimension of protein-detergent complexes, Phys. Rev. Lett. 57, 2583-2586.
11. Santos, S. F., Zanette, 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.
12. Carter, D. C., and Ho, J. X. (1994) Structure of serum albumin. Adv. Protein Chem. 45, 153-203.
13. Peters, T., Jr. (1985) Serum albumin, Adv. Protein Chem. 37, 161-245.
14. Brown, J. R. (1977) in Albumin Structure, Function, and Uses (Rosenoer, V. M., Oratz, M., and Rothschild, M. A., Eds.) pp 27-51, Pergamon, Oxford, U.K.
15. Peters, T. J. (1996) All about Albumin, Academic Press, San Diego.
16. Oncley, J. L., Scatchard, G., and Brown, A. (1947) Physicochemical characteristics of certain of the proteins of normal human plasma, J. Phys. Colloid Chem. 51, 184-198.
17. Tanford, C., and Buzzell, J. G. (1956) The viscosity of aqueous solutions of bovine serum albumin between pH 4.3 and 10.5. J. Phys. Chem. 60, 225-231.
18. Champagne, M. (1957) The structure of serum albumin in dilute solution. 1. Serum albumin at the isoionic point, J. Chim. Phys. 54, 378-392.
19. Squire, P. G., Moser, P., and O'Konski, C. T. (1968) Hydrodynamic properties of bovine serum albumin monomer and dimer, Biochemistry 7, 4261-4272.
20. Wright, A. K., Thompson, M. R., and Miller, R. L. (1975) A study of protein-sodium dodecyl sulfate complexes by transient electric birefringence, Biochemistry 14, 3224-3228.
21. Luzzati, V., Witz, J., and Nicolaieff, A. (1961) The structure of bovine serum albumin in solution at pH 5.3 and 3.6; study by absolute scattering of X-rays, J. Mol. Biol. 3, 379-392.
22. Bloomfield, V. (1966) The structure of bovine serum albumin at low pH, Biochemistry (Moscow) 5, 684-689.
23. Feng, L., Hu, C. Z., and Andrade, J. D. (1988) Scanning tunneling microscopic images of adsorbed serum albumin on highly oriented pyrolytic graphite, J. Colloid Interface Sci. 126, 650-653.
24. Ferrer, M. L., Duchowicz, R., Carrasco, B., Garcia de la Torre, J., and Acuna, A. U. (2001) The conformation of serum albumin in solution: A combined phosphorescence depolarization-hydrodynamic modeling study. Biophys. J. 80, 2422-2430.
25. He, X. M., and Carter, D. C. (1992) Atomic structure and chemistry of human serum albumin. Nature 358, 209-215.
26. Jones, M. N., Skinner, H. A., and Tipping, E. (1975) The interaction between bovine serum albumin and surfactants, Biochem. J. 147, 229-234.
27. Geisow, M. J., and Beaven, G. H. (1977) Physical and binding properties of large fragments of human serum albumin, Biochem. J. 163, 477-484.
28. Khan, M. Y. (1986) Direct evidence for the involvement of domain III in the N-F transition of bovine serum albumin. Biochem. J. 236, 307-310.
29. Takeda, K., Moriyama, Y., and Hachiya, K. (2002) in Encyclopedia of Surface and Colloid Science (Hubbard, A. T., and Somasundaran, P., Eds.) pp 2558-2574, Marcel Dekker, New York.
30. Hayashita, T., Kurosawas, T., Miyata, T., Tanaka, K., and Igawa, M. (1994) Effect of structural variation within cationic azosurfactant upon photoresponsive function in aqueous solution, Colloid Polym. Sci. 272, 1611-1619.
31. Shin, J. Y., and Abbott, N. L. (1999) Using light to control dynamic surface tensions of aqueous solutions of water soluble surfactants, Langmuir 15, 4404-4410.
32. Eastoe, J., Dominguez, M. S., Wyatt, P., Beeby, A., and Heenan, R. K. (2002) Properties of a stilbene-containing gemini photo-surfactant: Light-triggered changes in surface tension and aggregation. Langmuir 18, 7837-7844.
33. Eastoe, J., Sanchez-Dominguez, M., Cumber, H., Burnett, G., Wyatt, P., and Heenan, R. K. (2003) Photoresponsive microemulsions, Langmuir 19, 6579-6581.
34. Shang, T., Smith, K. A., and Hatton, T. A, (2003) Photoresponsive surfactants exhibiting unusually large, reversible surface tension changes under varying illumination conditions, Langmuir 19, 10764-10773.
35. Lee, C. T., Smith, K. A., and Hatton, T. A. (2004) Photoreversible viscosity changes and gelation in mixtures of hydrophobically-modified polyelectrolytes and photosensitive surfactants, Macromolecules 37, 5397-5405.
36. Glinka, C. J., Barker, J. G., Hammouda, B., Krueger, S., Moyer, J. J., and Orts, W. J. (1998) The 30 m small-angle neutron scattering instruments at the National Institute of Standards and Technology, J. Appl. Crystallogr. 31, 430-445.
37. Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria, J. Appl. Crystallogr. 25, 495-503.
38. Bendedouch, D., and Chen, S. H. (1983) Structure and interparticle interactions of bovine serum albumin in solution studied by small-angle neutron scattering, J. Phys. Chem. 87, 1473-1477.
39. Mittelbach, P., and Porod, G. (1962) Small-angle X-ray scattering of dilute colloids. VII. Distribution functions of triaxial ellipsoids, Acta Phys. Austriaca 15, 122-147.
40. Feigin, L. A., and Svergun, D. I. (1987) Structure Analysis by Small-Angle X-ray and Neutron Scattering, Plenum Press, New York.
41. Bergstrom, M., and Skov Pedersen, J. (1999) Structure of pure SDS and DTAB micelles in brine determined by small-angle neutron scattering (SANS), Phys. Chem. Chem. Phys. 1, 4437-4446.
42. Hayter, J. B., and Penfold, J. (1981) An analytic structure factor for macroion solutions, Mol. Phys. 42, 109-118.
43. Hansen, J. P., and Hayter, J. B. (1982) A rescaled MSA structure factor for dilute charged colloidal dispersions, Mol. Phys. 46, 651-656.
44. Sharma, R. V., and Sharma, K. C. (1977) The structure factor and the transport properties of dense fluids having molecules with square well potential, a possible generalization, Physica A 89, 213-218.
45. Tardieu, A., Le Verge, A., Malfois, M., Bonnete, F., Finet, S., Ries-Kautt, M., and Belloni, L. (1999) Proteins in solution: From X-ray scattering intensities to interaction potentials, J. Cryst. Growth 196, 193-203.
46. Heller, W. T., Krueger, J. K., and Trewhella, J. (2003) Further insights into calmodulin-myosin light chain kinase interaction from solution scattering and shape restoration, Biochemistry 42, 10579-10588.
47. Oh, Y. S., and Johnson, C. S., Jr. (1981) The wave vector dependence of diffusion coefficients in photon correlation spectroscopy of protein solutions, J. Chem. Phys. 74, 2717-2720.
48. Gaigalas, A. K., Hubbard, J. B., McCurley, M., and Woo, S. (1992) Diffusion of bovine serum albumin in aqueous solutions. J. Phys. Chem. 96, 2355-2359.
49. Takeda, K., Sasaoka, H., Sasa, K., Hirai, H., Hachiya, K., and Moriyama, Y. (1992) Size and mobility of sodium dodecyl sulfate-bovine serum albumin complex as studied by dynamic light scattering and electrophoretic light scattering. J. Colloid Interface Sci. 154, 385-392.
50. Chen, A., Wu, D., and Johnson, C. S., Jr. (1995) Determination of the binding isotherm and size of the bovine serum albumin-sodium dodecyl sulfate complex by diffusion-ordered 2D NMR. J. Phys. Chem. 99, 828-834.
51. Meechai, N., Jamieson, A. M., and Blackwell, J. (1999) Translational diffusion coefficients of bovine serum albumin in aqueous solution at high ionic strength, J. Colloid Interface Sci. 218, 167-175.
52. Valstar, A., Almgren, M., Brown, W., and Vasilescu, M. (2000) The interaction of bovine serum albumin with surfactants studied by light scattering, Langmuir 16, 922-921.
53. Kirkwood, J. G. (1954) The general theory of irreversible processes in solutions of macromolecules, J. Polym. Sci. 12, 1-14.
54. Bloomfield, V. A., Dalton, W. O., and van Holde, K. E. (1967) Frictional coefficients of multisubunit structures. I. Theory, Biopolymers 5, 135-148.
55. Slayter, E. M. (1965) An electron microscope study of the conformational change in bovine serum albumin at low pH. J. Mol. Biol. 14, 443-452.
56. Nozaki, Y., Reynolds, J. A., and Tanford, C. (1974) Interaction of a canonic detergent with bovine serum albumin and other proteins, J. Biol, Chem. 249, 4452-4459.
57. Kaneshina, S., Tanaka, M., Kondo, T., Mizuno, T., and Aoki, K. (1973) Interaction of bovine serum albumin with detergent cations. Bull. Chem. Soc. Jpn. 46, 2735-2738.
58. Glatter, O. (1977) A new method for the evaluation of small-angle scattering data, J. Appl. Crystallogr. 10, 415-421.
59. Svergun, D. I., Petoukhov, M. V., and Koch, M. H. J. (2001) Determination of domain structure of proteins from X-ray solution scattering, Biophys. J. 80, 2946-2953.
60. Sjoeberg, B., and Mortensen, K. (1997) Structure and thermodynamics of nonideal solutions of colloidal particles: Investigation of salt-free solutions of human serum albumin by using small-angle neutron scattering and Monte Carlo simulation. Biophys. Chem. 65, 75-83.
61. Kiselev, M. A., Gryzunov lu, A., Dobretsov, G. E., and Komarova, M. N. (2001) Size of a human serum albumin molecule in solution, Biofizika 46, 423-427.
62. Velev, O. D., Kaler, E. W., and Lenhoff, A. M. (1998) Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen, Biophys. J. 75, 2682-2697.
63. Ninio, J., Luzzati, V., and Yaniv, M. (1972) Comparative small-angle X-ray scattering studies on unacylated, acylated, and crosslinked Escherichia coli transfer RNAIVa1, J. Mol. Biol. 71, 217-229.
64. Timchenko, A. A., Ptitsyn, O. B., Dolgikh, D. A., and Fedorov, B. A. (1978) The structure of ribonuclease in solution does not differ from its crystalline structure, FEBS Lett. 88, 105-108.
65. Fedorov, B. A., and Denesyuk, A. I. (1978) Large-angle X-ray diffuse scattering, a new method for investigating changes in the conformation of globular proteins in solutions, J. Appl. Crystallogr. 11, 473-477.
66. Pavlov, M. Y., Sinev, M. A., Timchenko, A. A., and Ptitsyn, O. B. (1986) A study of apo- and holo-forms of horse liver alcohol dehydrogenase in solution by diffuse X-ray scattering. Biopolymers 25, 1385-1397.
67. Heidorn, D. B., and Trewhella, J. (1988) Comparison of the crystal and solution structures of calmodulin and troponin C, Biochemistry 27, 909-915.
68. Durchschlag, H., and Zipper, P. (1996) Comparative determination of structural parameters and conformational changes of proteins by small-angle scattering, crystallography, and hydrodynamic analysis, J. Mol. Struct. 383, 223-229.
69. Tanford, C. (1950) Preparation and properties of serum and plasma proteins. XXIII. Hydrogen-ion equilibria in native and modified human serum albumins, J. Am. Chem. Soc. 72, 441-451.
70. Hunter, M. J. (1966) A method for the determination of protein partial specific volumes, J. Phys. Chem. 70, 3285-3292.
71. Kuntz, I. D., Jr., and Kauzmann, W. (1974) Hydration of proteins and polypeptides, Adv. Protein Chem. 28, 239-345.
72. Stenstam, A., Montalvo, G., Grille, I., and Gradzielski, M. (2003) Small angle neutron scattering study of lysozyme-sodium dodecyl sulfate aggregates, J. Phys. Chem. B 107, 12331-12338.
73. Lee, C. T., Smith, K. A., and Hatton, T. A. (2004) Small-angle neutron scattering (SANS) studies of photosensitive surfactant-polyelectrolyte gels, in progress.
74. Vasilescu, M., Angelescu, D., Almgren, M., and Valstar, A. (1999) Interactions of globular proteins with surfactants studied with fluorescence probe methods, Langmuir 15, 2635-2643.
75. Brown, J. R., and Scockley, P. (1982) in Lipid-Protein Interactions (Jost, P. C., and Griffith, O. H., Eds.) pp 25-68. Wiley, New York.
76. Sarkar, N., Das, K., Nath, D. N., and Bhattacharyya, K. (1994) Twisted charge-transfer processes of Nile Red in homogeneous solutions and in faujasite zeolite, Langmuir 10, 326-329.
77. Dutta, A. K., Kamada, K., and Ohta, K. (1996) Spectroscopic studies of Nile Red in organic solvents and polymers, J. Photochem. Photobiol., A 93, 57-64.
78. Sackett, D. L., and Wolff, J. (1987) Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces, Anal. Biochem. 167, 228-234.
79. Daban, J. R., Samso, M., and Bartolome, S. (1991) Use of Nile Red as a fluorescent probe for the study of the hydrophobic properties of protein-sodium dodecyl sulfate complexes in solution, Anal. Biochem. 199, 162-168.
80. Santra, M. K., Banerjee, A., Krishnakumar, S. S., Rahaman, O., and Panda, D. (2004) Multiple-probe analysis of folding and unfolding pathways of human serum albumin. Evidence for a framework mechanism of folding. Eur. J. Biochem. 271, 1789-1797.
81. Jönsson, B., Lindman, B., Holmberg, K., and Kronberg, B. (1998) in Surfactants and Polymers in Aqueous Solutions, pp 219-245. Wiley, New York.