I am very skeptical about reports of miraculous elixirs. In all ages, there were expensive elixirs, which allegedly were cured of diseases. Here is a link to the method for getting rid of amyloid plaques: http://www.kurzweilai.net/method-discovered-to-remove-damaging-amyloid-plaques-found-in-alzheimers-disease I advise you to be more careful about optimistic articles about help with Alzheimer's disease. Please, reference: http://brainblogger.com/2006/03/04/studies-embryonic-stem-cells-as-a-cure-for-alzheimers-disease/ First of all, it is necessary to understand the mechanisms of this pathology. Then a method of prevention and therapy will be found. Please see the Attachment with scientific articles on this issue.

Actually, for this question I am not referring to "miraculous elixirs" but chemical reactions in vitro that could be targeted to amyloid plaques based on their unique makeup.

I remember Goethe, who figuratively said in Faust - "Dry theory is my friend, but the tree of life is green." Are you sure that the results you get in vitro will be useful for in vivo use? From my point of view, it is more promising to search for pathological mechanisms that lead to the formation of plaques, since the knowledge of such mechanisms will help clinicians prevent the development of Alzheimer's diseases. On the other hand, your right to study any other hypothesis. I wish you good luck.

Hi Kong, very interesting question. EPPS structurally similar to taurine has shown to amyloid beta plague in mice. Verubecestat has also showed to dissolve amyloid beta plague in small phase 1trial. Following link might help you... Thanks

Newly discovered protein shown to cause amyloid-beta plaques in Alzheimer's

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Oct 2 2018

Researchers have known for many years that amyloid-beta protein slowly builds up in the brain, and form plaques that lead to neuronal cell death and eventually, Alzheimer’s disease (AD).

Now, scientists have discovered that a potassium channel called KCNB1 can trigger the formation of amyloid-beta plaques.

📷Image Credit: Juan Gaertner / Shutterstock

The results of a new study titled, Oxidation of KCNB1 channels in the human brain and in a mouse model of Alzheimer’s disease, were recently published in the journal Cell Death & Disease.

The study showed that when the brain is under stress, there is a build up of KCNB1. This protein is toxic to the brain’s nerve cells and triggers the production of amyloid-beta.

In the study, the build-up of activated KCNB1 channels was associated with levels of free radicals.

Indeed, scientists have known for a long time that during aging or in neurodegenerative disease cells produce free radicals. Free radicals are toxic molecules that can cause a reaction that results in lost electrons in important cellular components, including the channels.” Professor Federico Sesti, Study Co-author

Sesti added that KCNB1 is oxidated and accumulates in the brain.

He noted that most Alzheimer’s disease studies do not go beyond laboratory mice into humans, but this protein has also been studied in humans so the evidence is conclusive.

He went on to say that this protein did not only play a role in Alzheimer’s disease but also minor brain trauma.

The protein has been found to play a role in inflammatory changes in the brain and in this study, was shown to trigger the deposition of the amyloid beta protein plaques.

This study provides the first experimental evidence that oxidative modification of KCNB1 takes place in the aging human brain and is exacerbated in the Alzheimer’s brain. KCNB1 oxidation, cause neuroinflammation, amyloidosis, and cognitive impairment.”

Source:

Oxidation of KCNB1 channels in the human brain and in a mouse model of Alzheimer’s disease

Thanks a lot, Marianne! I wonder if there are potentially more than one type of ion channels other than this one which may be discovered in the near future! Pieces of puzzle showing up...

Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design

• Qin Cao,
• Woo Shik Shin,
• Henry Chan,
• Celine K. Vuong,
• Bethany Dubois,
• Binsen Li,
• Kevin A. Murray,
• Michael R. Sawaya,
• Juli Feigon,
• Douglas L. Black,
• David S. Eisenberg &
• Lin Jiang

Nature Chemistry (2018) | Download Citation

Abstract

Inhibiting the interaction between amyloid-β (Aβ) and a neuronal cell surface receptor, LilrB2, has been suggested as a potential route for treating Alzheimer’s disease. Supporting this approach, Alzheimer’s-like symptoms are reduced in mouse models following genetic depletion of the LilrB2 homologue. In its pathogenic, oligomeric state, Aβ binds to LilrB2, triggering a pathway to synaptic loss. Here we identify the LilrB2 binding moieties of Aβ (16KLVFFA21) and identify its binding site on LilrB2 from a crystal structure of LilrB2 immunoglobulin domains D1D2 complexed to small molecules that mimic phenylalanine residues. In this structure, we observed two pockets that can accommodate the phenylalanine side chains of KLVFFA. These pockets were confirmed to be 16KLVFFA21 binding sites by mutagenesis. Rosetta docking revealed a plausible geometry for the Aβ–LilrB2 complex and assisted with the structure-guided selection of small molecule inhibitors. These molecules inhibit Aβ–LilrB2 interactions in vitro and on the cell surface and reduce Aβ cytotoxicity, which suggests these inhibitors are potential therapeutic leads against Alzheimer’s disease.