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The Effect of Surface-Bound FXIII-A Crosslinking on Fibrin Deposition, Structure and Mechanics
Abstract
Factor XIII (FXIII) plays a crucial role in maintaining hemostasis by crosslinking fibrin, thus stabilizing blood clots. Specifically, the active form, FXIII-A, enhances the mechanical properties of clots. This study aims to investigate the role of surface-immobilized FXIII-A in the structure and mechanics of fibrin networks. We hypothesize that surface-bound FXIII-A increases fibrin network density and stiffness through crosslinking interactions, compared to uncrosslinked fibrin networks bound to the surface. To achieve this, first we will characterize fibrin network formation on FXIII-A-coated microspheres by quantifying fibrin deposition kinetics using fluorescence microscopy, examining fibrin fiber morphology with Scanning Electron Microscopy, and assessing the impact of plasma FXIII-A on fibrin deposition dynamics. We noticed that FXIII-A on the surface increases the fibrin deposition, length of fibrin fibers, and decreases the curvature of the fibers. Next, we will elucidate the mechanical properties of fibrin networks crosslinked by surface FXIII-A by characterizing their response to shear stress and evaluating the role of FXIII-A in enhancing fibrin network stability and resistance to mechanical deformation. We observed that surface-bound FXIII-A increases the shear stiffness and contractility of the network as a whole. Overall, our results provide insights into the contributions of surface-bound FXIII-A to the structural and mechanical of fibrin networks.
