Scientists use a mathematical model to map how toxic proteins cluster in the brain in the early stages of dementia. Treatment of Alzheimer’s disease Have used. Read the details of the news below.
Researchers from the University of York’s School of Physics, Engineering and Technology say this discovery could have important implications for the treatment of Alzheimer’s disease and other similar diseases, commonly known as dementia. The results of this research in the journal Frontiers in Molecular Neuroscience It’s been published.
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What causes Alzheimer’s and how can Alzheimer’s be treated?
The study showed that most of the proteins involved in Alzheimer’s disease – called amyloids – turn into dense clumps of fluid before forming clusters that affect normal brain activity. So the way Treatment of Alzheimer’s disease Knowing the function of this protein.
As you may know, Alzheimer’s disease is the most common form Dementia It affects more than 50 million people worldwide, and it is predicted that this number will triple by 2050, which is something around 150 million people, which is a significant number.
Anatomy of Alzheimer’s disease
At the nanoscale, toxic amyloid proteins accumulate in the brain about 10 to 15 years before the first symptoms of the disease appear, but we still do not know how and how this phenomenon occurs. In the near future, by understanding precisely how protein clusters form, scientists may be in a much better position to develop targeted drug treatments to prevent the formation of these amyloids.
In this regard, Dr. Steve Quinn, a British Alzheimer’s researcher and a biophysics lecturer at the University of York, said:
“Understanding the precise molecular mechanisms by which amyloid clusters form will likely help us design better anti-amyloid cluster drugs that will reverse Alzheimer’s disease.”
The first stage of the fight against Alzheimer’s
We found that the same methods previously used to understand the growth of spider webs could be applied to our understanding of amyloid clustering. At this point, our work provides theoretical support for the so-called amyloid hypothesis, and helps explain the phenomenon under which conditions these clusters are formed.
In this study, scientists looked at two types of amyloid protein, both of which are widely found in the disease. They found that proteins may first form droplets in the stationary phase – so-called liquid-liquid phase separation condensates; This step precedes the formation of clusters enriched with the longer and more toxic version of this protein.
We believe that amyloid proteins are an important part of the body’s immune system, but when they are abnormally deformed, they accumulate in important biological structures, and their accumulation in the structures can interfere with the normal activities of the brain; For example, they disrupt brain functions by perforating cells or by affecting the behavior of important biomolecules.
Dr. Quinn and Shaffer, from the Department of Biophysics, are using experimental and theoretical tools to learn more about important issues involved in the biology of human disease.
Charlie Schaefer, research associate professor at York University and lead author of the study, said:
“The properties of large pre-formed clusters have been studied in great detail, but so far, only molecular chain-level details have been addressed in their early stages, making assessment difficult.”
He added: “We hope that our approaches can be useful for understanding the building blocks of many other forms of dementia, including Parkinson’s and Huntington’s.” “Because the idea that proteins form liquid-like droplets before aggregating into clusters may not be unique to Alzheimer’s disease and may be more common than previously thought.”
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