2008 Woodie Awards
UIC chemists characterize Alzheimer's neurotoxin structure
Kate Lee
Issue date: 2/18/08 Section: Pulse
Associate professor of Chemistry Yoshitaka Ishii and his team have isolated an intermediate structure of the fiber-like amyloid plaques (fibrils) which, they believe, can be responsible for the nerve cell damage associated with Alzheimer's. Although there is much research required to discover the causes and treatments for this disease, Ishii and his research team of chemists have put forward a new approach to the treatment, and perhaps even the prevention of Alzheimer's.
The degenerative disease known as Alzheimer's is said to be caused by a build-up of proteins in the brain. Amyloid plaques - fiber-like proteins - contribute to this build-up, leading to nerve cell death. The destruction of these nerve cells contributes to the trademark memory loss and other neurological malfunctions that are associated with Alzheimer's.
According to the Alzheimer's Association, amyloid plaques are an overabundance of protein deposits, and in the case of Alzheimer's, it is a buildup of misfolded amyloid proteins. Proteins take up different configurations, sheet-folding being one of them. However, the accumulation of misfolded amyloid proteins somehow contributes to nerve cell degeneration.
"It is not completely understood how the amyloid proteins are formed," said Ishii. "Somehow the small protein called amyloid is overly produced in the brain, and then they form the fibril structure which is extended and pointed in shape."
The final amyloid fibril was then compared to the intermediate structure, which the team discovered has a rich molecular structure in a spherical shape in its early stages, averaging around 20 nanometers in diameter.
Ishii explained that "the spheres eventually assemble into the final fibril amyloid structure." This transitional form of the protein has been found to be more toxic than the mature fibril itself. The final fibrils composed of amyloid-beta proteins trigger nerve cell damage and death, yet the intermediate spherical structures that Ishii and his team have isolated are 10 times more toxic to nerve cells. The team confirmed this by comparing the toxicity of the final amyloid protein to that of the intermediary's.
The degenerative disease known as Alzheimer's is said to be caused by a build-up of proteins in the brain. Amyloid plaques - fiber-like proteins - contribute to this build-up, leading to nerve cell death. The destruction of these nerve cells contributes to the trademark memory loss and other neurological malfunctions that are associated with Alzheimer's.
According to the Alzheimer's Association, amyloid plaques are an overabundance of protein deposits, and in the case of Alzheimer's, it is a buildup of misfolded amyloid proteins. Proteins take up different configurations, sheet-folding being one of them. However, the accumulation of misfolded amyloid proteins somehow contributes to nerve cell degeneration.
"It is not completely understood how the amyloid proteins are formed," said Ishii. "Somehow the small protein called amyloid is overly produced in the brain, and then they form the fibril structure which is extended and pointed in shape."
The final amyloid fibril was then compared to the intermediate structure, which the team discovered has a rich molecular structure in a spherical shape in its early stages, averaging around 20 nanometers in diameter.
Ishii explained that "the spheres eventually assemble into the final fibril amyloid structure." This transitional form of the protein has been found to be more toxic than the mature fibril itself. The final fibrils composed of amyloid-beta proteins trigger nerve cell damage and death, yet the intermediate spherical structures that Ishii and his team have isolated are 10 times more toxic to nerve cells. The team confirmed this by comparing the toxicity of the final amyloid protein to that of the intermediary's.
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