Researchers from University of Rochester Medical Centre have made subtle changes in the structure of a key protein that may help in developing new treatments for hemophilia, an inherited blood disorder.
Hemophilia is caused by a lack of a protein, factor VIII, one of several proteins in a chain reaction that enables blood to solidify, or clot, to plug wounds after injury.
By making subtle changes in the protein, the researchers have been able to dramatically increase its ability to drive blood clotting.
Current preventive treatment consists of genetically engineered factor VIII administered by injection, but one quarter of those born with no factor VIII suffer severe immune reactions that render the treatment inactive. In addition, current treatment costs as much as 200,000 dollars per patient per year.
The team led by Philip Fay, Ph.D., professor in the Department of Biochemistry and Biophysics at the University of Rochester Medical Centre has identified key amino acids with the potential, if replaced, to change the performance of entire protein.
"Our goal is to improve upon nature by developing gain-of-function factor VIII proteins that are superior to the version of the 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. On the other hand, we have sought to change the protein's structure as little as possible, because the immune system is more likely to react the more we change it," he added.
The study is published in Journal of Thrombosis and Hemostasis.