Research and practice in thrombosis and haemostasis · 2026
A novel biosensor for measuring plasmin activity.
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Dai Ying, Kim Paul Y, Heitmeier Stefan, Weitz Jeffrey I, Gross Peter L
Аннотация
BACKGROUND: Plasmin facilitates fibrinolysis by catalyzing the degradation of fibrin clots. Reliable methods to assess fibrinolysis by measuring plasmin generation are needed in the preclinical and clinical settings.
OBJECTIVES: This study aimed to design, synthesize, and evaluate a fluorescence resonance energy quenching-based plasmin sensor (FPS) protein to monitor plasmin generation.
METHODS: The hydrolysis of FPS was monitored by loss of fluorescence resonance energy quenching to evaluate efficiency and specificity. Plasma-based plasmin generation assays were used to evaluate fibrinolytic cofactors and inhibitors.
RESULTS: Compared with a peptide plasmin sensor, FPS demonstrated higher efficiency for plasmin and was not cleaved by plasmin inhibited by α2-macroglobulin. FPS interacts with plasmin's kringle domain 5. FPS can measure plasmin generation in clotting plasma, which was increased by an inhibitory antibody against α2-antiplasmin and attenuated by aprotinin, tranexamic acid, and fibrin absence. Maximal plasmin generation occurs after peak clot formation. Furthermore, when antiplasmin is inhibited, the presence of plasminogen activator inhibitor-1 can be measured. Unlike peptide sensors, FPS does not inhibit clot lysis. Lastly, plasmin generation measured using FPS is relatively consistent in plasma from healthy volunteers, with only a 2-fold variation in peak plasmin, peak time, and endogenous plasmin potential.
CONCLUSION: FPS may improve the evaluation of fibrinolysis in preclinical and clinical settings, thereby enhancing our understanding of fibrinolytic disorders.
OBJECTIVES: This study aimed to design, synthesize, and evaluate a fluorescence resonance energy quenching-based plasmin sensor (FPS) protein to monitor plasmin generation.
METHODS: The hydrolysis of FPS was monitored by loss of fluorescence resonance energy quenching to evaluate efficiency and specificity. Plasma-based plasmin generation assays were used to evaluate fibrinolytic cofactors and inhibitors.
RESULTS: Compared with a peptide plasmin sensor, FPS demonstrated higher efficiency for plasmin and was not cleaved by plasmin inhibited by α2-macroglobulin. FPS interacts with plasmin's kringle domain 5. FPS can measure plasmin generation in clotting plasma, which was increased by an inhibitory antibody against α2-antiplasmin and attenuated by aprotinin, tranexamic acid, and fibrin absence. Maximal plasmin generation occurs after peak clot formation. Furthermore, when antiplasmin is inhibited, the presence of plasminogen activator inhibitor-1 can be measured. Unlike peptide sensors, FPS does not inhibit clot lysis. Lastly, plasmin generation measured using FPS is relatively consistent in plasma from healthy volunteers, with only a 2-fold variation in peak plasmin, peak time, and endogenous plasmin potential.
CONCLUSION: FPS may improve the evaluation of fibrinolysis in preclinical and clinical settings, thereby enhancing our understanding of fibrinolytic disorders.