How the key toxic protein of Alzheimer's disease is formed, new research points out the importance of acid-base environment

For decades, many people concerned about Alzheimer's disease have focused their attention on amyloid beta (Aβ)

According to the Aβ theory and the support of many research evidences, small-scale aggregates composed of a small amount of Aβ, namely Aβ oligomers, are very toxic to nerve synapses and are the only cause of Alzheimer’s disease.

Recently, a research team in Germany explored the formation conditions of Aβ oligomers

Research results show that the formation of Aβ oligomers is closely related to pH

Endosomes and lysosomes are two small vesicle structures in cells, which play a key role in the process of material transport and degradation

"Now, our results show that endosomes and lysosomes are also places where Aβ oligomers are preferentially formed

▲Endosomes and lysosomes are the key sites that affect Aβ assembly in cells (picture source: reference [1])

The researchers also observed that with the increase of toxic Aβ oligomers, the mislocalization of another protein, tau, appeared in nerve cells, a protein closely related to the progression of Alzheimer's disease

▲Aβ oligomer (picture source: reference [2]; Credit: Forschungszentrum Jülich, HHU Düsseldorf / Wolfgang Hoyer)

In addition, the research team analyzed the size and composition of Aβ oligomers through cryo-EM and AFM

Note: The original text has been deleted

Reference materials:

[1] Marie P.

[2] New insights into the formation of toxic protein clumps in Alzheimer's disease.

Retrieved Aug.