It can prevent nervous diseases

pte20240404012 Research/Development, Medical/Health

According to American researchers, changing one amino acid works against the accumulation of tau proteins.

Brain scan: diseases need to be cured as soon as possible (photo: pixabay.com, Dmitriy Gutarev)

Brain scan: diseases need to be cured as soon as possible (photo: pixabay.com, Dmitriy Gutarev)

Santa Barbara (pte012/04.04.2024/10:30)

Neurodegenerative diseases such as frontotemporal dementia, progressive supranuclear palsy, and corticobasal degeneration can be diagnosed by misfolded tau proteins. It is a collection of abnormal proteins in the brain. A group University of California Santa Barbara Kenneth S. With Kozik, Kenneth has now found ways to interrupt this process. To do this, they target “sticky” points with elongated mutant tethers, thereby preventing neurofibrillary tangles from misfolding and spreading.

Diseases are different

Tau is considered a fundamental structural protein in the brain, giving cells shape and stability and helping transport essential nutrients. However, if this protein mutates and misfolds, it can become sticky and form clumps. This folding error becomes a template for misfolding, which accumulates until normal tau proteins misfold and spread to vast areas of the brain, affecting function.

Depending on which neurodegenerative disease it is, the specific areas where neurofibrillary tangles develop also differ. There are two specific forms of tau that act as the starting point for this type of neurodegenerative disease. Among the so-called taupathies, Alzheimer's disease is considered the most well-known disease. Tau produced a shorter “three-repeat” version and a longer “four-repeat” version. The present study focuses on the longer version. Rarer taupathies than Alzheimer's disease are exclusively type 4R diseases.

Camel Nanobodies

Using sophisticated techniques such as transmission electron microscopy and molecular dynamics simulations with cell cultures, researchers have gained insight into the conditions under which pathological 4R-Tau begins to misfold. According to Kosik, tau folds in a unique way in each of these diseases. “One region folds into a hairpin structure only in 4R-tau. Through this hairpin, an adhesive region called PHF6 can bind other tau proteins to form large aggregates,” it says.

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According to experts, replacing a single amino acid with a protein near the adhesive region is enough to prevent tau accumulation. The nanobodies, i.e. fragments of antibodies synthesized from the blood of camels, were able to bind to the PHF6 region, preventing the accumulation of tau. This knowledge is the first big step toward new treatments for neurodegenerative diseases. However, it takes a long time for them to actually be used. Details are published in the journal “Proceedings of the National Academy of Sciences”.

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