Protein prof tackles sticky plaque

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On June 13, 2011

A Missouri S&T chemical engineer is doing his part to prevent or cure neurological diseases like Alzheimer’s, Parkinson’s or Mad Cow. These diseases all have one common element — amyloid plaque deposits. But they are all made up of different proteins.

Daniel Forciniti

Daniel Forciniti is working to stop neurological diseases like Alzheimer’s. (Photo by B.A. Rupert)

Daniel Forciniti, professor of chemical and biological engineering, and his team are working to find a way to make various proteins create amyloid deposits in conditions that mimic the human body. Through the study, the researchers are also working to better understand what types of structures encourage plaque formation.
Nearly 15 years ago, Forciniti’s group began studying how proteins and peptides behave when they are near a solid surface — such as when a protein in blood is near the inner surface of a vein. “We have developed considerable expertise in both theoretical and experimental studies of proteins at solid-liquid interfaces,” he says. “The transition to the study of the effect of surfaces, such as tissue, on the formation of protein aggregates was a natural one.”

While the debate over what causes these diseases continues, it’s commonly accepted that an abnormal buildup of these protein deposits on the surface of the brain, also known as amyloid deposits or plaques, are found in people with Alzheimer’s disease.

Scientists have been able to trick proteins into creating amyloid plaques, but only in extremely acidic and high-temperature environments. That situation is vastly different from what occurs in the human body, Forciniti says.

“They subject these proteins to harsh conditions at unrealistically high concentrations,” Forciniti says. For example, these proteins may be immersed in a 3 pH solution, significantly more acidic than a human body’s pH of 7.5. Instead of using nanomoles of peptides, as is found in the brain, millimoles of peptides are used.

Forciniti and his colleagues are working to develop a way to create these proteins in an environment that is closer to that of the human body.

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On June 13, 2011. Posted in Research, Summer 2011