Surfactant-induced amorphous aggregation of tobacco mosaic virus coat protein: A physical methods approach

Macromolecular Bioscience

Volumn 8, Issue 2, 2008, Pages 199-209

  Panyukov, Yuliy V ^a   Nemykh, Maria A ^a   Dobrov, Eugeny N ^a   Drachev, Vladimir A ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Aggregation; Calorimetry; Dynamic light scattering; Proteins; Surfactants

Indexed keywords

AGGREGATES; AGRICULTURAL PRODUCTS; ANIONIC SURFACTANTS; CALORIMETERS; CALORIMETRY; COLLOIDS; CONCENTRATION (PROCESS); CRITICAL MICELLE CONCENTRATION; DIFFERENTIAL SCANNING CALORIMETRY; DYES; DYNAMIC LIGHT SCATTERING; ELECTROMAGNETIC WAVES; FLOW INTERACTIONS; IONIC STRENGTH; LASER INTERFEROMETRY; LIGHT SCATTERING; MICELLES; REFRACTION; SODIUM; SODIUM SULFATE; SURFACE ACTIVE AGENTS; TOBACCO; VIRUSES; VOLUMETRIC ANALYSIS;

AGGREGATION; AMORPHOUS; AMORPHOUS AGGREGATIONS; COAT PROTEINS; CRITICAL AGGREGATION CONCENTRATIONS; DYNAMIC LIGHT; HYDROPHOBIC; IONIC SURFACTANTS; ISOTHERMAL TITRATION CALORIMETRIES; MIXED MICELLES; PARTIAL DENATURATIONS; PHYSICAL METHODS; PROTEIN AGGREGATIONS; PROTEIN COMPLEXES; PROTEIN MOLECULES; SODIUM DODECYL SULFATES; STOICHIOMETRIC RATIOS; SURFACTANTS; TOBACCO MOSAIC VIRUS COAT PROTEINS; TOBACCO MOSAIC VIRUSES; TRITON X-100;

AGGLOMERATION;

COAT PROTEIN; DODECYL SULFATE SODIUM; NONIONIC SURFACTANT; TRITON X 100; CAPSID PROTEIN; OCTOXINOL; SURFACTANT;

ARTICLE; CHEMICAL INTERACTION; CONCENTRATION RESPONSE; DIFFERENTIAL SCANNING CALORIMETRY; HYDROPHOBICITY; IONIC STRENGTH; ISOTHERMAL TITRATION CALORIMETRY; LIGHT SCATTERING; NONHUMAN; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN INTERACTION; PROTEIN SECRETION; STOICHIOMETRY; TOBACCO MOSAIC VIRUS; TURBIDIMETRY; CHEMISTRY; COMPARATIVE STUDY; METHODOLOGY; MICELLE; PHOTOMETRY; PHYSICAL CHEMISTRY;

TOBACCO MOSAIC VIRUS;

CALORIMETRY, DIFFERENTIAL SCANNING; CAPSID PROTEINS; CHEMISTRY, PHYSICAL; MICELLES; NEPHELOMETRY AND TURBIDIMETRY; OCTOXYNOL; SODIUM DODECYL SULFATE; SURFACE-ACTIVE AGENTS; TOBACCO MOSAIC VIRUS;

EID: 41249095351     PISSN: 16165187     EISSN: 16165195     Source Type: Journal    
DOI: 10.1002/mabi.200700145     Document Type: Article

References (57)

1. A. L. Fink, Folding Des. 1998, 3, R9.
2. C. M. Dobson, Trends Biochem. Sci. 1999, 24, 329.
3. S. Lovestone, D. M. McLoughlin, J. Neurol., Neurosurg, Psychiatry 2001, 72, 152.
4. J. D. Wood, T. P. Beaujeux, P. J. Shaw, Neuropathol, Appl. Neurobiol. 2003, 29, 529.
5. B. Nolting, "Protein Folding Kinetics", Springer-Verlag, Berlin Heidelberg New York 1999.
6. i. N. Shalova, R. A. Asryants, M. V. Sholukh, L. Saso, B. i, Kurganov, V. I. Muronetz, V. A. Izumrudov, Macromol., Biosci. 2005, 5, 1184.
7. K. A. Markossian, B. I. Kurganov, D. I. Levitsky, H. A. Khanova, N. A. Chebotareva, A. M. Samoilov, T. B. Eronina, N. V, Fedurkina, A. M. Mitskevich, A. V. Meremyanin, S. Y. Kleymenov, V. F. Makeeva, V. I. Muronetz, I. N. Naletova, I. N. Shalova, R. A. Asryants, E. V. Schmalhausen, L. Saso, Y, V. Panyukov, E. N. Dobrov, I. K. Yudin, A. C. Timofeeva, K. O. Muranov, M. A. Ostrovsky, "mechanism of Chaperone-Like Activity", in: Protein Folding: New Research, T. R. Obalinsky, Ed., Nova Science, New York 2006, p. 89.
8. T. L McMeekin, B. D. Polis, E. S. DellaMonica, J. H. Custer, J. Biol. Chem. 1949, 71, 3606.
9. A. K. Moren, k Khan, Langmuir 1995, 11, 3636.
10. S. Ghosh, A. Banerjee, Biomacromolecules 2002, 3, 9.
11. C. Sun, J. Yang, X. Wu, X. Huang, F. Wang, S. Liu, Biophys. J. 2005, 88, 3518.
12. T. Considine, H. Singh, H. A. Patel, L K. Creamer, J. Agric. Food Chem. 2005, 53, 3197.
13. T. A. Pertinhez, M. Bouchard, R. A. G. Smith, C. M. Dobson, L. J. Smith, FEBS Lett. 2002, 529, 193.
14. M. Bisaglia, I. Tessari, L. Pinato, M. Bellanda, S. Giraudo, M. Fasano, E. Bergantino, L. Bubacco, S. Mammi, Biochemistry 2005, 44, 329.
15. M. F. Ahmad, T. Ramakrishna, B. Raman, C. M. Rao, J. Mol. Biol. 2006, 364, 1061.
16. J. Butler, J. Gen. Virol. 1984, 65, 253.
17. R. Diaz-Avalos, D. L. Caspar, J. Mol. Biol. 2000, 279, 67.
18. V. N. Orlov, A. M. Arutyunyan, S. V. Kust, E. A. Litmanovich, V. A. Drachev, E. N. Dobrov, Biochemistry (Moscow) 2001, 66, 154.
19. E. R. Rafikova, B. I. Kurganov, A. M. Arutyunyan, S. V. Kust, V. A. Drachev, E. N. Dobrov, Int. J. Biochem. Cell Biol. 2005, 35, 1452.
20. K. Namba, R. Pattanayek, G. Stubbs, J. Mol. Biol. 1989, 208, 307.
21. E. R. Rafikova, Y. V. Panyukov, A. M. Arutyunyan, L. S. Yaguzhinsky, V. A. Drachev, E. N. Dobrov, Biochemistry (Moscow) 2004, 69, 1372.
22. Y. V. Panyukov, M. A. Nemykh, E. R. Rafikova, B. I. Kurganov, L. S. Yaguzhinsky, A. M. Arutyunyan, V. A. Drachev, E. N. Dobrov, Int. J. Biochem. Cell Biol. 2006, 38, 533.
23. T. W. Randolph, L. S. Jones, Pharm. Biotechnol. 2002, 13, 159.
24. S. D. Webb, J. I. Cleland, J. F. Carpenter, T. W. Randolph, J. Pharm. Sci. 2003, 92, 715.
25. D. K. Chou, R. Krishnamurthy, T. W. Randolph, J. F. Carpenter, M. C. Manning, Pharm. Sci. 2005, 94, 1368.
26. J. C. Pan, J. S. Wang, Y. Cheng, Z. Yu, X. M. Rao, H. M. Zhou, Biochem. Cell Biol. 2005, 83, 140.
27. M. Abu-Eid, S. V. Kust, I. V. Makeeva, V. K. Novikov, E. N. Dobrov, Mol. Genet., Mikrobiol. Virusol. 1994, 3, 28.
28. B. I. Kurganov, E. R. Rafikova, E. N. Dobrov, Biochemistry (Moscow) 2002, 67, 525.
29. Y. V. Panyukov, E. R. Rafikova, E. N. Dobrov, Dokl. Biochem. Biophys. 2005, 402, 258.
30. Y. V. Panyukov, I. K. Yudin, V. A. Drachev, E. N. Dobrov, B. I. Kurganov, Biophys. Chem. 2007, 127, 9.
31. H. Fraenkel-Conrat, Virology 1957, 1, 1.
32. E. N. Dobrov, S. V. Kust, O. Y. Yakovleva, T. Tikhonenko, Biochim. Biophys. Acta 1977, 475, 623.
33. V. N. Orlov, S. V. Kust, P. V. Kalmykov, V. P. Krivosheev, E. N. Dobrov, V. A. Drachev, FEBS Lett. 1998, 433, 307.
34. M. L. Collins, M. R. Salton, Biochim Biophys. Acta 1979, 553, 40.
35. H. A. Khanova, K. A. Markossian, B. I. Kurganov, A. Samoilov, S. Y. Kleimenov, D. I. Levitsky, I. K. Yudin, A. Timofeeva, K. O. Muranov, M. A. Ostrovsky, Biochemistry 2005, 44, 15480.
36. K. A. Markossian, H. A. Khanova, S. Y. Kleimenov, D. I. Levitsky, N. A. Chebotareva, R. A. Asryants, V. I. Muronets, L. Saso, I. K. Yudin, B. I. Kurganov, Biochemistry 2006, 45, 13375.
37. H. A. Khanova, K. A. Markossian, S. Y. Kleimenov, D. I. Levitsky, N. A. Chebotareva, N. V. Golub, R. A. Asryants, V. I. Muronetz, L. Saso, I. K. Yudin, K. O. Muranov, M. A. Ostrovsky, B. I. Kurganov, Biophys Chem. 2007, 125, 521.
38. D. Weitz, J. Huang, M. Lin, J. Sung, Phys. Rev. Lett. 1985, 54, 1416.
39. D. Weitz, M. Lin, Phys. Rev. Lett. 1986, 57, 2037.
40. M. Lin, H. Linsday, D. Weitz, R. Ball, R. Klein, P. Meakin, Proc. R. Soc. London A 1989, 423, 71.
41. M. Berka, J. A. Rice, Langmuir 2005, 21, 1223.
42. M. Anson, J. Gen. Physiol. 1939, 23, 239.
43. E. L. Duggan, F. M. Luck, J. Biol. Chem. 1948, 172, 205.
44. K. Shirahama, K. Tsujii, T: Takagi, J. Biochem. 1974, 75, 309.
45. N. J. Turro, X. Lei, K. P. Ananthapadmanabhan, M. Aronson, Langmuir 1995, 11, 2525.
46. R. K. Jain, W. T. Chang, C. Geetha, P. B. M. Joyce, S. U. Gorr, Biochem. J. 2002, 368, 605.
47. S. Tandon, P. Horowitz, J. Biol. Chem. 1986, 261, 15615.
48. S. Tandon, P. Horowitz, J. Biol. Chem. 1990, 265, 5967.
49. D. Rozema, S. H. Gellman, J. Biol. Chem, 1996, 271, 3478.
50. D. L. Daugherty, D. Rozema, P. E. Hanson, S. H. Gellman, J. Biol. Chem. 1998, 273, 3961.
51. P. Dutta, A. Halder, S. Mukherjee, P. Sen, S. Sen, K. Bhattacharyya, Langmuir 2002, 18, 7867.
52. H. Diamant, D. Andelman, Macromolecules 2000, 33, 8050.
53. S. Guillot, M. Delsanti, S. Dersert, D. Langevin, Langmuir 2003, 19, 230.
54. D. M. Zhu, R. K. Evans, Langmuir 2006, 22, 3735.
55. C. N. Chirita, M. Necula, J. Kuret, J. Biol. Chem. 2003, 278, 25644.
56. M. Necula, C. N. Chirita, J. Kuret, J. Biol. Chem. 2003, 278, 46674.
57. C. N. Chirita, J. Kuret, Biochemistry 2004, 43, 1704.