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by JumpCrisscross 3320 days ago
Would it be encouraging to see if amyloid plaques dissolve in a concentrated aqueous solution of ATP? (Sorry if nonsensical. I am approaching the topic as a layman.)
1 comments

Had a different response here before but this quote from the article suggests maybe!

"ATP kept proteins in boiled egg white from aggregating."

It also appears the concentrations they're talking about are quite reasonable (10mM or so).

That said, once an aggregate is formed you usually need pretty heroic methods to solubilize it. Much stronger detergents and denaturants at higher must be used, and in those cases you run into other problems.

After solubilizing the aggregate, you have to fold the individual proteins back up. But now you have to do it in an environment where you 1.) a molecule that keeps the protein unfolded and 2.) a ton of other unfolded proteins around. You could slowly get rid of 1.) by dialysis or something similar. But when you have a bunch of unfolded proteins hanging around together, you almost always get aggregates.

In practice, it's quite unlikely that ATP concentrations high enough to unfold an aggregate wouldn't unfold all sorts of other things. This would also mean the stuff you need to keep the rest of the cell working... so from a practical perspective this is unlikely to work.