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

cases buried charged amino acids were replaced by non-charged substitutes. While they found several of the single mutations doubled the stability of factor VIII, and of factor VIIIa, certain combinations of mutations increased stability by up to ten times, suggesting synergy between the mutations. Another benefit of this approach is that any changes to the structure are buried within the protein, so they would not attract notice by the blood-based immune system that might react to them.

Specifically, Fay and Wakabayashi found three amino acids (Asp519, Glu665, and Glu1984) located in the interfaces between the A2 domain with domains A1 and A3, were reducing the strength of the attraction between the domains because of their charges. Their removal via mutations increased factor VIII thermal stability by 200 percent and its chemical stability by 30 percent increase. It reduced the ability of A2 to break away from factor VIIIa by 800 percent, and brought about an increase in thrombin generation capacity of 220 percent.

"Moving forward, we are excited about this line of work because we have identified further changes that promise the engineering of an even more stable factor VIII, and we now have designed a version of the protein that combines increased stability with better calcium binding for increased activity, a version that pharmaceutical companies are starting to show interest in," Fay said. "Our goal from these redesigns remains to prolong the treatment effect, make it less expensive and lessen the chances of rejection by the immune system."


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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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