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