Efanesoctocog alfa elicits functional clot formation that is indistinguishable to that of recombinant factor VIII.

ABSTRACT:

Background

Factor VIII (FVIII) binding to endogenous von Willebrand factor (VWF) has constrained half-life extension of recombinant FVIII (rFVIII) products for hemophilia A. Efanesoctocog alfa (rFVIIIFc-VWF-XTEN; BIVV001) is a novel fusion protein designed to decouple FVIII from VWF in circulation and maximize half-life prolongation by XTEN^® polypeptides and Fc fusion. FVIII, VWF, and platelets interact to achieve normal hemostasis. Thus, bioengineered FVIII replacement products, such as efanesoctocog alfa, require comprehensive assessment of their hemostatic potential.

Objectives

We compared functional clot formation and injury-induced platelet accumulation between efanesoctocog alfa and rFVIII.

Patients/methods

The hemostatic potential of efanesoctocog al

SUBMITTER: Demers M 

PROVIDER: S-EPMC9320793 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature