Anomalous mechanics of Zn2+-modified fibrin networks.

Jing Xia, Li-Heng Cai, Huayin Wu, Frederick C MacKintosh, David A Weitz

Proceedings of the National Academy of Sciences of the United States of America 2021 Mar 09

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Fibrin is the main component of blood clots. The mechanical properties of fibrin are therefore of critical importance in successful hemostasis. One of the divalent cations released by platelets during hemostasis is Zn2+; however, its effect on the network structure of fibrin gels and on the resultant mechanical properties remains poorly understood. Here, by combining mechanical measurements with three-dimensional confocal microscopy imaging, we show that Zn2+ can tune the fibrin network structure and alter its mechanical properties. In the presence of Zn2+, fibrin protofibrils form large bundles that cause a coarsening of the fibrin network due to an increase in fiber diameter and reduction of the total fiber length. We further show that the protofibrils in these bundles are loosely coupled to one another, which results in a decrease of the elastic modulus with increasing Zn2+ concentrations. We explore the elastic properties of these networks at both low and high stress: At low stress, the elasticity originates from pulling the thermal slack out of the network, and this is consistent with the thermal bending of the fibers. By contrast, at high stress, the elasticity exhibits a common master curve consistent with the stretching of individual protofibrils. These results show that the mechanics of a fibrin network are closely correlated with its microscopic structure and inform our understanding of the structure and physical mechanisms leading to defective or excessive clot stiffness.

Citation

Jing Xia, Li-Heng Cai, Huayin Wu, Frederick C MacKintosh, David A Weitz. Anomalous mechanics of Zn2+-modified fibrin networks. Proceedings of the National Academy of Sciences of the United States of America. 2021 Mar 09;118(10)