Studies have shown that Alzheimer's disease is caused by the accumulation of abnormal spiral protein deposits in the brain, but little is known about the molecular structure of these so-called β-amyloid fibers.
Recently, a group of researchers from the NIH of the National Institutes of Health announced a new result, revealing that the different molecular structure of β-amyloid fiber may be determined by different clinical history and different brain damage in Alzheimer's disease degree. This discovery will help to develop new treatments and improve the diagnosis and treatment of this common disease.
Corresponding author of the article is the National Institutes of Health Robert Tycko, who said, "This work is the first to describe in detail the molecular structure of β-amyloid fiber, which is a key cause of Alzheimer's "Protein", "Relevant detailed structural models can be used to guide the development of compounds that can bind to this protein with high specificity, for diagnostic imaging, but also for the development of drugs that inhibit protein formation, prevention and treatment of Alzheimer's Silent disease. "
Alzheimer's disease AD is a chronic neurodegenerative disease that occurs worldwide, mainly in middle-aged and elderly people. With the aging of the population, the incidence of AD is increasing. A recognized feature of this degenerative disease of the central nervous system characterized by progressive cognitive impairment is amyloid deposition.
Tycko and his research team have previously found that β-amyloid fibers grown in petri dishes have different molecular structures, and different structures depend on specific growth conditions. Based on this observation, they suggested that the fibrin found in the brains of Alzheimer's patients may also be variable. These structural changes may be related to the clinical history of each patient. But for a long time, researchers have been unable to directly study the structure of this protein in the brain with low protein abundance.
To overcome this problem, Tycko and his colleagues developed a new experimental protocol-they extracted β-amyloid fiber fragments from the brain tissues of two patients with different clinical histories and degrees of brain damage, and then Using these fragments, a large number of fibers are cultivated in a petri dish. As a result, the researchers found that each patient has a high amount of single fibers in the brain tissue, and these molecular structures vary between patients.
"This may mean that a protein that appears to be in a single location in the brain in the patient may be dispersed to other locations and maintain the same molecular structure," Tycko said. "Our study also showed that certain proteins Compared with other structures, the fiber structure is more likely to cause Alzheimer's disease, which shows the importance of developing imaging reagents. With these reagents, we can target special fiber structures and improve the reliability and specificity of diagnosis. "
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