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Relationship between Fibrin Clot Structure and Fibrinogen and Thrombin Concentrations

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title
Relationship between Fibrin Clot Structure and Fibrinogen and Thrombin Concentrations
author
Zhang, Zezhong
abstract
Fibrinogen is one of the most abundant proteins in human blood plasma. In the event of an injury to the vasculature, thrombin proteolytically cleaves two pairs of fibrinopeptides off fibrinogen, and thereby converts it to fibrin. Fibrin polymerizes into fibrin fibers, which form a mesh that stabilizes a blood clot. This process plays an important role in thrombosis and hemostasis. In this research, we explored the relationship between structural properties (fiber density, pore size and fractal dimension) of a fibrin clot and concentrations of fibrinogen and thrombin. We also explored the effect of fibrinogen types - purified fibrinogen and fibrinogen in plasma - on fibrin structural properties. Confocal microscopy is the imaging technique we used in this research. We discovered that increasing fibrinogen concentrations, and increasing thrombin concentrations resulted in clots with higher fiber density, smaller pore size and higher fractal dimension. Clots formed from purified PEAK1 fibrinogen, instead of plasma fibrinogen, also showed higher fiber density, smaller pore size and higher fractal dimension. Based on these results, we found power law equations that relate structural properties to fibrinogen and thrombin concentrations. The equations indicate that fibrinogen concentration has a stronger effect on clot structure than thrombin concentration. We discuss implications of these results for clot formation, future research directions, and the importance of our results to thrombosis and hemostasis.
contributor
Bonin, Keith (advisor)
Carlson, Eric D (committee member)
date
2024-02-13T09:36:06Z (accessioned)
2023 (issued)
degree
Physics (discipline)
embargo
2025-02-12 (terms)
2025-02-12 (liftdate)
identifier
http://hdl.handle.net/10339/102907 (uri)
language
en (iso)
publisher
Wake Forest University
type
Thesis

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