Altering Fibrin Structure and Polymerization Dynamics Using Unaltered and PEGylated Fibrin Knob Peptides

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Aboujamous, Nader
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The behavior of the fibrin network in the presence of unaltered and PEGylated fibrin knob peptides is unknown. Fibrinogen, the principle protein investigated, participates in the coagulation cascade during hemostasis. Once activated by thrombin, it is converted to fibrin, which catalyzes Factor XIII to create a covalently cross-linked network. Fibrin knob peptides bind to the fibrin pockets and block polymerization, altering the mechanical properties of the resulting network. This study focuses on visualizing and analyzing confocal microscopy images to coordinate fibrin structure in the presence of peptides during polymerization. Using self-prepared and treated PDMS microfluidic devices, the solutions are mixed, injected, and imaged in real-time. The data is evaluated based on the calculated gel area fractions from 3D-rendered confocal images. The growth rates and maximal area of the fibrin networks are quantified and compared among the image sets. Data is used to predict how peptides alter the structure, development, and rate of fibrin network formation. Qualitatively, the incorporation of peptides into the fibrin matrix provides thicker fibers at lower overall network densities as compared to the control. The results show that fibrin knob peptides decrease the extent of network growth and that PEGylated peptides enhance this effect. A further understanding of peptides’ effects on the fibrin network structure will have a strong impact by leading to an enhancement of the biological activity of fibrin and expanding the scope of applications of the fibrin scaffold
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Undergraduate Thesis
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