Development of monomeric fibrin molecules to enable rationally-designed fibrin targeting strategies

Fibrin networks act as scaffolds for blood clots, but fibrin depositions are also linked to pathological conditions such as cardiovascular disease. Fibrin only differs by a few N-terminal amino acids from its soluble precursor fibrinogen, so differentiating between physiological and pathological fibrin depositions and differentiating between fibrin and fibrinogen are crucially important for correct clinical diagnoses and accurate therapeutic delivery. Because fibrin polymerizes upon its formation, it is inaccessible to traditional structural biology techniques, leaving structural differences between fibrinogen and fibrin unidentified.In this project, I will develop and validate a monomeric fibrin (mon-fibrin) construct to enable high-resolution structural studies. The development of monomeric fibrin was a sub-aim of a recently submitted NIH R15 proposal (Ramses # 19-0659). Data collected from this project will serve as preliminary evidence for an R15 re-submission if the first attempt is not funded or will be utilized to submit a larger NIH R01 proposal.

Scholars @ ECU