Their aim is to understand the detailed assembly process for the toxic protein called amyloid plaque. Such basic understanding, they said, could lead to approaches to preventing plaque formation.
The researchers led by Boris Akhremitchev are using the infinitesimal tip of a customized atomic force microscope (AFM) to capture, isolate and study single molecules, called monomers, that are the building blocks of the toxic protein polymers known as amyloid fibrils. Atomic force microscopes use a sharp microscopic tip to image surfaces and detect energy differences by mechanically probing molecular surfaces.
In a poster presentation at the American Chemical Society's annual meeting, the researchers will describe the first biophysical analysis of interactions between monomers that form the amyloid fibrils associated with Parkinson's disease.
This presentation will include studies by Chad Ray, a graduate student in Akhremitchev's research group, that clarify the nature of binding forces between amyloid molecules. The poster session will take place March 16, 2005, 7:30 - 10 p.m. Pacific Standard Time, in Hall D of the San Diego Convention Center.
This work was funded by the Camille and Henry Dreyfus Foundation and by Duke University.
It has been difficult to study the chemistry of formation of these fibrils within the brains of humans and other animals, said Akhremitchev, who is an assistant professor of chemistry.
In the brain, "monomers of all kinds are suspended in a soup in equilibrium," he said. Given that the components of amyloid fibrils measure only billionths of a meter and are floating in a disordered mix, "the initial stages of amyloid aggregation are not