Abstract
The noncovalent immobilization of the protein bovine serum albumin on the surface of spherical nanoparticles 330 ± 60 nm in diameter is described. These nanoparticles are prepared by the thermal treatment of tobacco mosaic virus and are preliminarily covered with a layer of the cationic polymer poly(N-ethyl-4-vinylpyridinium bromide). The electrostatic adsorption of the polycation on the surface of negatively charged spherical nanoparticles (on average 1.2 × 104 macromolecules per particle) is accompanied by recharging of the surface; as a result, the negatively charged protein bovine serum albumin can be adsorbed on it in an amount of 1.7 × 104 molecules per particle. The modification of spherical nanoparticles with the polycation and protein does not cause the aggregation of particles. The spherical-nanoparticle-polycation-protein ternary complex demonstrates increased stability in salt solutions relative to the spherical-nanoparticle-polycation binary complex. Because of the simplicity of the method used to modify the surface of spherical nanoparticles, it shows promise for preparation of functionally active complexes.
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References
J. Atabekov, N. Nikitin, M. Arkhipenko, et al., J. Gen. Virol. 92, 453 (2011).
A. Klug, Philos. Trans. R. Soc. 354, 531 (1999).
R. A. Williams and H. W. Blanch, Biosens. Bioelectron. 9, 159 (1994).
J. Turkova, J. Chromotogr. B 722, 11 (1999).
A. S. Malinin, A. A. Rakhnyanskaya, A. V. Bacheva, and A. A. Yaroslavov, Polymer Science, Ser. A 53, 52 (2011) [Vysokomol. Soedin., Ser. A 53, 54 (2011)].
S. A. Sukhishvili, O. S. Chechik, and A. A. Yaroslavov, J. Colloid Interface Sci. 178, 42 (1996).
V. K. Novikov and J. G. Atabekov, Virology 41, 101 (1970).
K. G. Mann and W. W. Fish, Methods Enzymol. 26, 28 (1972).
P. G. Seybold, M. Gouterman, and J. Callis, Photochem. Photobiol. 9, 229 (1969).
R. M. Fuoss and U. P. Strauss, J. Polym. Sci. 3, 246 (1948).
W. Ebeling, N. Hennrich, M. Klockow, et al., Eur. J. Biochem. 47, 91 (1974).
H. Fraenkel-Conrat and B. Singer, Philos. Trans. R. Soc. London 354, 583 (1999).
K. M. Smith and M. A. Lauffer, Adv. Virus Res. 13, 42 (1968).
Jr. B. W. Maidment, L. D. Papsidero, and T. M. Chu, J. Immunol. Methods 35, 297 (1980).
K. Y. Chun and P. Stroeve, Langmuir 18, 4653 (2002).
A. A. Yaroslavov, E. G. Yaroslavova, A. A. Rakhnyanskaya, et al., Colloid Surf. B 16, 29 (1999).
H. Fischer, I. Polikarpov, and A. F. Craievich, Protein Sci. 13, 2825 (2004).
D. A. Davydov, E. G. Yaroslavova, A. A. Efimova, and A. A. Yaroslavov, Kolloidn. Zh. 73, 512 (2008).
A. B. Zezin, V. B. Rogacheva, V. S. Komarov, and E. F. Razvodovskii, Vysokomol. Soedin., Ser. A 17, 2637 (1975).
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Original Russian Text © N.A. Nikitin, A.S. Malinin, A.A. Rakhnyanskaya, E.A. Trifonova, O.V. Karpova, A.A. Yaroslavov, J.G. Atabekov, 2011, published in Vysokomolekulyarnye Soedineniya, Ser. A, 2011, Vol. 53, No. 11, pp. 1885–1891.
This work was supported by the Russian Foundation for Basic Research (project no. 11-03-00936) and the federal target program Scientific and Educational Specialists of Innovation Russia (State Contracts 02.740.11.0789 and 02.527.11.0002).
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Nikitin, N.A., Malinin, A.S., Rakhnyanskaya, A.A. et al. Use of a polycation spacer for noncovalent immobilization of albumin on thermally modified virus particles. Polym. Sci. Ser. A 53, 1026–1031 (2011). https://doi.org/10.1134/S0965545X11110083
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DOI: https://doi.org/10.1134/S0965545X11110083