Abstract
Using the methods of dynamic and elastic light scattering and confocal laser scanning microscopy, the damage in the spatial fibrin structure during peroxide- and hypochlorite-induced oxidation of fibrinogen was studied. Peroxide had a weak effect on the structural organization of fibrin, whereas hypochlorite caused the formation of abnormal fibrin with reduced individual fiber diameter and decreased porosity. Measurements of the size distributions of the native and oxidized fibrinogen revealed a decrease in the hydrodynamic size of the oxidized fibrinogen molecule with an increase in the concentration of oxidizers. These results indicate that the hydrophobicity of fibrinogen surface increased and its colloidal stability decreased. The possible role of oxidative sites in the assembly of structurally abnormal fibrin is analyzed.
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