Use of a polycation spacer for noncovalent immobilization of albumin on thermally modified virus particles

• Published in: Polymer science. Series A, Chemistry, physics Vol. 53; no. 11; pp. 1026 - 1031
• Main Authors: Nikitin, N. A., Malinin, A. S., Rakhnyanskaya, A. A., Trifonova, E. A., Karpova, O. V., Yaroslavov, A. A., Atabekov, J. G.
• Format: Journal Article
• Language: English
• Published: Dordrecht SP MAIK Nauka/Interperiodica 01-11-2011
• Subjects: Adsorption; Chemistry; Chemistry and Materials Science; Polyelectrolytes; Polymer Sciences; Tobacco mosaic virus; Polymer Science Series; Bovine Serum Albumin Complex; Tobacco Mosaic Virus Particle; Spherical Nanoparticles; Tobacco Mosaic Virus
• ISSN: 0965-545X; 1555-6107
• DOI: 10.1134/S0965545X11110083

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 × 10
4
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 × 10
4
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.