FVII(1-211)-Fc

FVII(1-211)-Fc is a catalytically inactive, bivalent recombinant fusion protein designed to selectively modulate the initiation of the coagulation cascade. It is a rationally engineered construct consisting of the first 211 amino acids of Factor VII (FVII), which includes the domains responsible for binding to Tissue Factor (TF) but lacks the entire protease domain required for catalytic activity. This FVII fragment is fused to an engineered IgG1 Fc domain to enable dimerization and enhance molecular stability while minimizing effector functions. By binding to TF, FVII(1-211)-Fc acts as a competitive antagonist, preventing the formation of the functional TF-FVIIa initiation complex. This mechanism dose-dependently reduces TF-mediated Factor X activation and attenuates downstream thrombin generation without compromising baseline hemostasis. It is being investigated for the treatment of thromboinflammatory disorders, including sepsis, malignancy-associated coagulopathy, and disseminated intravascular coagulation (DIC).

Other names

catalytically inactive bivalent FVII-Fc fusion protein