Turoctocog Alfa (Recombinant Coagulation Factor VIII): A Comprehensive Clinical and Pharmacological Review

Section I: Molecular Architecture and Biochemical Characterization

1.1 The Bioengineered B-Domain Truncated Structure

Turoctocog alfa is a recombinant human coagulation factor VIII (rFVIII), a glycoprotein biopharmaceutical designed for the management of Hemophilia A.[1] Its defining molecular feature is a strategically truncated B-domain, a modification that distinguishes it from endogenous full-length Factor VIII (FVIII) and certain other recombinant products.[4] The B-domain of the native FVIII protein is a large, heavily glycosylated region comprising 908 amino acids that has been demonstrated to be largely dispensable for the protein's procoagulant activity.[5] The engineered structure of turoctocog alfa removes the majority of this domain, retaining a minimal linker of just 21 amino acids. This linker is composed of 10 amino acids from the N-terminus and 11 amino acids from the C-terminus of the naturally occurring B-domain.[3]