A forum should be a place of lively debate. In this spirit, one MUST pose the question, " who cares about amyloid fibrils?" For those of us seeking a cure for Alzheimer's disease (AD), we want to identify the proximate neurotoxin. The most popular current hypothesis is that oligomeric forms of the amyloid ?-protein (A?) are this neurotoxin. So, why waste time trying to understand what in essence is waste!?

What IS interesting is the conformational dynamics of a protein, A?, that populates such large volumes of conformational space and yet has the capacity to fold and oligomerize. How is this possible? Is this an emergent phenomenon? How do we answer these questions and what implications would the answers have, and for whom?

Anyone dare respond?

The most popular current hypothesis is that oligomeric forms of the amyloid ?-protein (A?) are this neurotoxin. So, why waste time trying to understand what in essence is waste!?

For one, it appears that these toxic oligomers are a step on the route to the formation of the waste amyloid material. If no one had tried to understand it, would we know what we know now about Alzheimer's? Also, could the pathway from oligomers to amyloid plaques have more easily identifiable species that would indicate the presence of such oligomers and thus assist with earlier detection of the disease?

For two, there are many serious human diseases that are linked by the presence of amyloid accumulations...perhaps understanding the entire pathway from A? to amyloid will help to uncover unifying principles in all of these diseases?

For three, amyloids are interesting all on their own, playing a role in many natural and novel materials....that have nothing to do with disease or Alzheimer's.

I could not have said it better myself! I'm just very surprised that it took this long for someone to respond to my comment.