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Redesigned protein accelerates blood clotting
Date:12/22/2008

stability) or detergents (chemical stability). In the case of factor VIII, stability measures the strength with which the other factor VIII domains hold on to the A2 domain, the piece most likely to break away. Inactive Factor VIII is converted into active Factor VIIIa by protein when clotting begins, but this cannot happen though if the A2 domain of factor VIII has already fallen off.

As pharmaceutical companies manufacture the current hemophilia treatment, recombinant factor VIII, the protein is grown in a cell culture, purified in several steps, freeze-dried to convert it into powder and added to saline before it can be injected into the body. A small but significant portion of the protein is unraveled or broken up during this bruising process, but a more durable version could mean the delivery of more active protein by the time it hits the body, researchers said. Furthermore, when more stable factor VIII is converted into factor VIIIa, the VIIIa cofactor better holds onto the A2 domain, which is the reason that the current study found that more stable mutants increase clotting.

In a recent paper in the journal Blood, the team used molecular biology techniques to swap out those three charged residues with residues that carried no charge, removing barrier to the closing attraction between factor VIII's domains. The fact that oil separates from water has been harnessed by life. Cells have oily barriers that keep out the watery world, and the insides of blood proteins like factor VIII "prefer" non-charged, oily interactions to carry out their functions. Of course, nature is not perfect, so some charged residues are buried within proteins, including within factor VIII domain interfaces.

In the current paper, the team compared the chemical and thermal stability of mutated forms of factor VIII containing one of the single mutations proved earlier to increase stability against mutant forms with combinations of the same mutations. In all
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Contact: Greg Williams
Greg_Williams@urmc.rochester.edu
585-275-3676
University of Rochester Medical Center
Source:Eurekalert

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