Summary
The prophylactic treatment of haemophilia B and the management of haemophilia A or
B with inhibitors demand frequent administrations of coagulation factors due to the
suboptimal half-lives of the products commercially available and currently in use,
e.g. recombinant factor IX (rFIX) and recombinant factor VIIa (rFVIIa), respectively.
The extension of the half-lives of rFIX and rFVIIa could allow for longer intervals
between infusions and could thereby improve adherence and clinical outcomes and may
improve quality of life. Albumin fusion is one of a number of different techniques
currently being examined to prolong the half-life of rFIX and rFVIIa. Results from
a phase I clinical trial demonstrated that the recombinant fusion protein linking
FIX to albumin (rIX-FP) has a five-times longer half-life than rFIX, and preclinical
studies with the recombinant fusion protein linking FVIIa to albumin (rVIIa-FP) suggest
that rVIIa-FP possesses a significantly extended half-life versus rFVIIa. In this
review, we describe albumin fusion technology and examine the recent progress in the
development of rIX-FP and rVIIa-FP.
keywords
Coagulation factor IX - coagulation factor VIIa - half-life extension - albumin fusion