Electric field affects alpha-synuclein aggregation
 

Alpha-synuclein is thought to play a role in the pathogenesis of PD. The problem is not simply a case of having too much alpha-synuclein, but rather a case of the misfolding of the protein leading to its aggregation.

Clearly, being able to control the aggregation would have theraputic implications.

In a paper published 5 years ago, Osawa et al. reported:

"The aggregation of alpha-synuclein without comformational change occurred rapidly when a voltage of 1V was applied."

Unfortunately, this is the opposite effect to that required.

Does anyone know of any later work in this area?

Tag johnt:alpha-synuclein

Reference

[1] "Aggregation and Fibrillation Study of alpha-synuclein Under Applied Voltage"
Osawa, et al.
Electrochemistry, 2008
https://www.jstage.jst.go.jp/article.../76_8_614/_pdf

Electrostatic interactions and α-synuclein fibrillation
 

I fund this abstract published July 30,2013 interesting:

"The hydrophobic and electrostatic interactions are associated with an increase in α-synuclein fibrillation propensity and that that the interpeptide hydrophobic interactions in the elongation of A53T α-synuclein protofilaments can be greatly weakened by trehalose. This suggests that trehalose inhibits the interpeptide interaction involved in protein secondary structure."

http://pubs.acs.org/doi/abs/10.1021/...nalCode=ancham

Trehalose
 

Trehalose is found in Life Enhancement's product called FoldRight.
Who knows? It might be helpful.

Here is the manufacturer's information:

Life extension scientists Durk Pearson & Sandy Shaw’s new nutritional drink mix, FoldRight™, helps to refold the proteins on which life depends, in ways that enhance health! FoldRight brings together what may be the most important natural chemical “chaperones” recognized to help achieve the proper form and function of your body’s proteins. FoldRight brings together what may be the most important natural chemical “chaperones” recognized to help achieve the proper form and function of your body’s proteins. FoldRight contains organic osmolytes, such as the amino acids proline, glycine, and beta-alanine, along with the nutrients inositol, betaine (trimethylglycine), taurine, and creatine, which are also osmolytes, and now the disaccharide trehalose, which is also an osmolyte. FoldRight goes where no nutritional formulation has ever gone before! Osmolytes are necessary for protein stability and to help maintain proteins in a correctly folded state. They preserve stability by keeping protein-denaturing ingredients (such as urea) away from the proteins’ surface, acting as chaperones to protect against contact with these denaturing agents, while not themselves interfering with protein/solvent (water) interactions. The osmolytes selected for the FoldRight “cocktail” are naturally found in living tissues in substantial quantities, are readily available, have been used safely in relatively large amounts as supplements or as components of foods for long periods of time, and are reasonably inexpensive." -