To change the direction of treatment of Alzheimer's disease

Researchers at the University of Lund, Sweden, used the latest technology to generate the formation of toxic clumps prior to β-amyloid. According to previous studies on recombinant rat proteins, β-amyloid is the root of Alzheimer's disease.

The scientific community has long believed that β-amyloid plaques are instantaneously present, and therefore the term "popcorn plaques" comes from it. However, the infrared spectrum shows the result is not the case.

"No one has used this method to observe the development of Alzheimer's disease," says Gunnar Gouras, professor of experimental neurology at Lund University. "These images tell us that progress in β-amyloid is slower than we thought and that Alzheimer's disease has a new understanding of the development process."

What does this discovery herald? Researchers use biochemical identification to see closer to Alzheimer's disease early brain changes. The results reveal another finding that β-amyloid is not a single peptide, which is linked together by four peptide units and exhibits a tetrameric form.

This finding provides a new hypothesis for the treatment of the disease - the abnormal separation of these four peptides may be the beginning of the accumulation of β -amyloid, followed by the formation of plaques. Another amyloid disease is associated with transthyretin amyloidosis, and tetrameric decomposition has been identified as the key to the development of the disease. For this disease, there is already a drug that stabilizes the tetramer, thereby stabilizing the β -amyloid protein for therapeutic purposes.

Thus, the finding can change the direction of our treatment of Alzheimer's disease. Most of the drugs are currently designed to eliminate plaques. Flarebio offers high-quality recombinant proteins like recombinant TLR2 at competitive prices.