Deposits of amyloid beta proteins in the brain are one of the defining characteristics of Alzheimer's disease. The prevention or reduction of such deposits is what researchers hope for in Alzheimer's disease research studies.

Researchers from NYU School of Medicine have reduced by around 50 percent the aggregation of toxic amyloid protein in the brains of mice by blocking the interaction between a protein called apolipoprotein E (apo E) and amyloid. (Apo E acts as a sort of biological chaperone, ferrying cholesterol and fats around the brain.)

"Our approach opens up a completely new avenue for therapy," says Dr. Wisniewski. "There is a lot of data showing that apo E is important in sporadic Alzheimer's disease. But until now no one has really addressed how you can manipulate its interaction with amyloid beta."

Alzheimer's affects some 4.6 million people in the United States, and the devastating neurodegenerative disease occurs most commonly as "sporadic," meaning it affects individuals who do not have rare genetic mutations.

Headed by Martin Sadowski, M.D., Ph. D., Assistant Professor of Neurology and Psychiatry and Dr. Thomas Wisniewski, M.D., Professor of Neurology, Pathology and Psychiatry, the research team created a nontoxic, synthetic protein fragment or peptide that binds to apo E, preventing it from latching onto amyloid. Once deprived of its biochemical chaperone, amyloid won't form deadly plaques.

The study results were published in the December 5, 2006 issue of the Proceedings of National Academy of Sciences.

Read more at NYU Med News.

[In photo: A brain slice from an 18-month-old transgenic mouse showing deposits of amyloid (yellow arrowhead) in brain tissue and in blood vessels (white arrowhead), Source: NYU Med]