Quote:
Originally Posted by johnt
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 |
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