Extending half-lives, cutting costs for proteins

NOTTINGHAM, U.K.—Novozymes recently signed an exclusive worldwide licensing agreement for its propriety albumin fusion technology, albufuse, with CSL Behring—a move that will help CSL Behring increase the circulatory half-life of a wide range of therapeutically relevant proteins.

The albufuse technology has been proven to extend the circulatory half-life of therapeutic proteins through genetic fusion to recombinant human albumin, Novozymes notes in a news release about the deal, something that could lead to increased bioavailability and therefore less frequent administration of drugs. Other potential benefits include reduced dosages and reduced side effects, and the technology may help development new therapies based on novel protein drugs, says Maree Devine, marketing communications manager for Novozymes.

While the fee for the license was not disclosed, both companies say it will enable CSL Behring to use albufuse technology for research, development and commercialization of novel biotherapeutic products. At this time, Novozymes has no information on potential financial impacts of the license deal.

"We have chosen Novozymes' albufuse as we believe it offers unique product and patient benefits to enhance our current protein therapeutic pipeline," says Val Romberg, senior vice president of R&D at CSL Behring. "As we recently presented at the meeting of the American Society of Hematology, results from recent preclinical studies are encouraging."

These data indicated that the fusion protein (rVIIa-FP) was shown to extend the half-life of the recombinant protein sixfold to ninefold compared to wild type (rFVIIa).

Additionally, rVIIa-FP demonstrated a biologic activity comparable to wild type rFVIIa. Recombinant factor VIIa (rFVIIa) is used to control bleeding episodes in hemophilia patients.

What that study did was show—for the first time—that it is feasible to genetically fuse FVIIa to human albumin, using albufuse, to prolong the half-life of this therapeutic protein while retaining its biologic activity, Devine says.