Baxter Healthcare Corporation has initiated a therapeutic programme for the development of a recombinant form of Von Willebrand Factor (VWF), a protein critical to the normal clotting of blood. Preclinical results presented suggest that a recombinant VWF therapeutic protein candidate has similar properties to plasma-derived VWF. ]
Data were presented at the American Society of Hematology (ASH) 48th annual meeting held December 9-12. Baxter will continue to conduct extensive preclinical research before the modified protein will be available for clinical evaluation.
"The initiation of this recombinant VWF therapeutic programme is an important strategic landmark as we build upon the success of our plasma/albumin-free platform," said Hartmut Ehrlich, MD., vice president, global research and development, for Baxter's BioScience business. "The majority of therapeutic clotting factors continue to be processed using blood-derived components. By applying Baxter's proven proprietary blood-free processing technology, we are working to develop a therapeutic option that will eliminate the potential risk of blood-borne pathogen transmission for people with von Willebrand disease."
Characterization of a Recombinant VWF Molecule at the ASH annual meeting, Baxter scientists presented initial data from experiments analysing several large-scale batches of recombinant VWF processed using the company's proprietary blood-free technology, which was subsequently purified. The properties of the purified recombinant proteins were then evaluated in comparison to three plasma-derived VWFs, including two commercially available therapeutic proteins.
According to these preliminary data, the recombinant VWF showed comparable properties to the plasma-derived proteins in the various biochemical evaluations, as well as similar pharmacokinetic properties in mouse models of von Willebrand disease. Overall, the results of these preclinical studies suggest that the properties of recombinant VWF both in vitro and in vivo are similar to those of plasma-derived VWF.