Abstract

The interaction between fibrinogen and magnetite nanoparticles in solution has been studied by the methods of spin labeling, ferromagnetic resonance, dynamic and Rayleigh light scattering. It was shown that protein molecules adsorb on the surface of nanoparticles to form multilayer protein covers. The number of molecules adsorbed on one nanoparticle amounts to approximately 65 and the thickness of the adsorption layer amounts to approximately 27 nm. Separate nanoparticles with fibrinogen covers (clusters) form aggregates due to interactions of the end D-domains of fibrinogen. Under the influence of direct magnetic field, nanoparticles with adsorbed proteins form linear aggregates parallel to force lines. It was shown that the rate of protein coagulation during the formation of fibrin gel under the action of thrombin on fibrinogen decreases approximately 2 times in the presence of magnetite nanoparticles, and the magnitude of the average fiber mass-length ratio grows.

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