Human fibrinogen is an important coagulation factor as well as an independent predictor of coronary heart disease and stroke. Analysis of dysfibrinogens may provide useful information and help us to understand the molecular defects in fibrin polymerization. In the present study, we investigated the influence of oxidative stress of fibrinogen induced by H2O2 on the polymerization state of fibrin. UV absorbance spectroscopy, circular dichroism, æ-potential, dynamic light scattering and steady shear viscosity were all employed to study the influence of oxidative stress on the molecular structure, the surface charges, and the size and shape of fibrinogen molecules. The fibrin morphology obtained was imaged and investigated using atomic force microscopy. The results demonstrated that the cross-linking, branching and height distribution of formed fibrin will be influenced by the oxidative stress of fibrinogen. This study presents new insights into the aggregation behaviour of fibrinogen and will be helpful to understand the formation mechanism of thrombosis under oxidative stress.
Circular Dichroism Fibrin