Interaction between blood plasma proteins and magnetite nanoparticles

Abstract

Spin label EPR spectroscopy and dynamic and Rayleigh light scattering are employed to study the interaction between magnetite nanoparticles with a diameter of 17 nm and plasma proteins (fibrinogen and albumin). Protein molecules are shown to be adsorbed on nanoparticle surface with the formation of multilayer shells. When a buffer solution (pH 8.5) contains 0.01 vol % nanoparticles, 90–100 fibrinogen molecules are adsorbed per one particle and the thickness of an adsorbed layer is 30–40 nm. For albumin, the layer thickness is 10–15 nm. In a constant magnetic field, large linear microsized aggregates oriented parallel to field lines are formed in dispersions of nanoparticles covered with adsorbed protein molecules. The study of fibrin gel formation resulting from the action of thrombin enzyme on fibrinogen suggests that, in the presence of nanoparticles, the rate of gelation decreases by a factor of approximately two, while the ratio between the average mass and average length of fibrin polymer fibers rises.