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Redesigned protein accelerates blood clotting

tissue. Calcium, a metallic element, must be present for factor VIII to work. Factor VIII has on its surface pocket-like chains of amino acids shaped to hold calcium ions (calcium binding sites). When calcium bonds to it, factor VIII changes shape and becomes better able to bind factor IX.

In past research, Fay's team had identified a single amino acid (out of the more than 2,300 building blocks making up factor VIII) with the potential, if replaced, to change the performance of entire protein. Researchers proved the theory in the current study by swapping out a glutamic acid naturally occurring at a specific point in a calcium binding site on factor VIII with 19 different amino acids. One of the replacements, alanine, doubled the ability of factor VIII to bind with factor IX. Results were measured by introducing each form of factor VIII into hemophilic blood plasma and recording the time it took to cause clotting.

Fay, along with Hironao Wakabayashi, M.D., a research assistant professor at the University of Rochester Medical Center and co-inventor, have filed a patent application for the factor VIII redesign used in the published study. Moving forward, Fay's team will target additional calcium binding sites with the goal of making changes that further increase factor VIII potency.

"Our goal is to improve upon nature by developing gain-of-function factor VIII proteins that are superior to the factor VIII protein found in healthy individuals," Fay said. "These more potent forms are not likely to occur naturally since they would theoretically result in excessive clotting, blocked arteries and heart attacks in otherwise healthy people. In patients with hemophilia, however, enhanced clotting is desirable."


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Source:University of Rochester Medical Center


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