Scientists discover... Water may play a key role in the spread of Alzheimer's within the brain

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A new study published in the journal PNAS and reported on the Science Alert website, and conducted by researchers from Northwestern and California Universities, revealed a potential mechanism that explains how the “tau” protein, which is linked to Alzheimer’s disease and other types of dementia, spreads, a discovery that may open the door to the development of treatments aimed at slowing the progression of the disease.

In the brains of people with Alzheimer's, amyloid-beta and tau proteins behave abnormally, but scientists are still studying whether these changes are a direct cause of the disease or a consequence of it.

The "tau" protein is one of the essential elements in this disease path, as it can take an abnormal shape and gather inside brain cells in the form of threads known as "fibrils", which ultimately leads to nerve cell damage and death.

The researchers were able to monitor what they described as the “active point” in tau proteins, which is a water-repellent area that helps the proteins bind to each other after the surrounding water molecules are released, beginning the process of forming solid fibrils associated with the deterioration of brain functions.

Sunji Han, a professor of physical chemistry at Northwestern University, said that this area cannot be completely covered by water molecules due to its water-repellent nature, but these molecules form a stable shell that protects the protein and helps it interact with other similar proteins.

The researchers explained that the formation of fibrils requires precise alignment of tau proteins with a distorted structure. When any imbalance occurs in this alignment, the growth of fibrils stops. Experiments also showed that covering the “active point” with a chemical marker prevents the continued formation of these protein structures.

This discovery is of particular importance because it indicates a potential therapeutic target that could be targeted with drugs in the future. Instead of dealing with the final consequences of the disease, it may be possible to disrupt a key step that allows tau to spread from one nerve cell to another.

When cells containing fibrils die, these structures are released into the surrounding environment and transmitted to other nerve cells, where the process repeats itself and contributes to the spread of the disease across different areas of the brain.

Han believes that identifying the site responsible for initiating the clumping process gives scientists an opportunity to disrupt the improper folding of the tau protein and prevent its transmission, which may contribute in the future to reducing the development of Alzheimer's and some forms of dementia.

The researchers also proposed developing artificial tau fibrils to study the stages of the disease with more precision, stressing that a deep understanding of how these structures form represents an essential step towards creating more effective treatments for neurodegenerative diseases.