Some scientists have developed a new approach that directly fights the development of neurological degenerative diseases, such as Alzheimer’s and atrophic lateral sclerosis. The researchers used nanoparticles coated with sugar to detain toxic proteins and prevent them from affecting nerve cells.
This approach was developed by researchers from the University of Northwestern in the United States, and the results of their studies were published in the Journal of the American Chemical Society on May 14 and wrote about the Yurrick Alert website.
Siege
Proteins are incorrectly intertwined and clog around the brain cells in degenerative neurological diseases, which ultimately leads to cell death. The innovative new treatment is surrounded by these proteins effectively before the formation of toxic structures capable of penetrating neurons. Then the besieged proteins in the body decompose without any harm.
This strategy greatly reinforced the survival of human neurons cultivated in the laboratory under the pressure of pathogenic proteins around them.
Samuel I said. Stop, pioneering researcher in the field of renewal medicine from the University of North Western who led the study, “Our study highlights the promising potential of nanoparticles, molecularly to treat the root causes of degenerative neurological diseases.” “In many of these diseases, proteins lose their folded functional structure and collect to form destructive fibers that enter nerve cells and are very toxic to them. By holding folded proteins wrongly, our treatment is confirming the formation of these fibers in an early stage. It is believed that the short amyloid fibers, which penetrate neurons, are the most toxic compositions in the early stage. It is with more work, this can be greatly delayed the development of the disease. “
The nanoparticles are fibers with a diameter of 1 and 100 nm. They are widely used in various vital medical applications, such as medication.
Trealose
According to the World Health Organization, up to 50 million people around the world may suffer a denial nervous disorder. Most of these diseases are characterized by the accumulation of deformed proteins in the brain, which leads to a gradual loss of neurons. While current treatments provide limited benefit, there is still an urgent need for new treatments.
To counter this challenge, the researchers have resorted to a group of dual -enforceable peptide amphiphiles, which contain modified chains of amino acids. Binary familiar peptides are already used in some well -known drugs, including Simaglotide (Ozmbek).
“The advantage of peptide -based medications is that they decompose into nutrients,” Stop said.
Over the years, the Stop Research Team has designed many peptide -based materials for various therapeutic purposes. To develop bi -familiar bityded to treat neurological degenerative diseases, his team added an additional component: a natural sugar called Trehalose.
“There is naturally in plants, fungi and insects, and it protects them from temperature changes, especially drought and freezing. Researchers have discovered that Truez can protect many large biomus molecules, including proteins. Therefore, we wanted to know if we can use it to install the irreplaceable proteins in a way correct”.
Instability is the basis
Dual -familiar peptides combine themselves when adding to water to form a nanopathic fiber wrapped in Trealose. Surprisingly, the Trealose is the stability of nanoparticles. Although this may seem illogical, this stability deficiency had a positive effect.
The nanopolitan fibers themselves are characterized by strength and good organization, and resistance to rearrange their structure. This is difficult for other molecules, such as non -folded proteins, fiber mergers. On the other hand, the fibers are less stable, more dynamic, and more likely to find and interact toxic proteins.
“The unstable gatherings of very interactive molecules. They want to interact with other molecules and link them. If the nanoparticles were stable, I would have ignored everything around them with pleasure,” Stop said.
The nanoparticles have been associated with amyloid-beta proteins in search of stability, and amyloid-beta proteins are the main cause of Alzheimer’s disease. However, the nanopolitan fibers not only prevented the amyloid-beta proteins from the bloc, but also combined it into its own fibrous structure, besieging them permanently into stable strands.
“So, the fibers are no longer a bilateral peptide, but rather a new hybrid structure that includes both dual-familiar peptide and amyloid-beta protein. This means that the bita-beta proteins, which would have formed the amyloid fibers, have become besieged. It is no longer able to penetrate and eliminate neurons. It is like a cleaning team of deformed proteins.”
To assess the therapeutic capabilities of the new approach, scientists conducted laboratory tests using human neurons derived from stem cells. The results showed that the nanoscopic fibers coated with Trehalaz significantly improved the nerve cells when exposed to the bita -toxa amyloid protein.
Stop says the new approach to using unstable nanoparticles to detain proteins provides a promising way to develop new and effective treatments for Alzheimer’s disease, atrophic side sclerosis and other degenerative neurological conditions.
“Our treatment may be more effective when targeting diseases at an early stage, before entering the gathered proteins into the cells. But it is difficult to diagnose these diseases in their early stages. Therefore, it can be combined with treatments targeting symptoms of late stages of the disease. Then, treatment may be a double blow,” Stop added.