For those who think of amyloid fiber formation as a prion-like process, you may want to review a paper I published (Xu, 2007). You can send your comments directly to me, e-mail shaohua@fit.edu, or comment on this forum. It seems to me that we are ignoring the work of a much larger group of scientists, chemists, and physicists.

I copy here the abstract: “Protein amyloid fibers are often found to have a β-pleated sheet structure regardless of their sequence, leading some to believe that it is the molecule’s misfolding that leads to aggregation. In this article, an alternative model is introduced for the amyloid community to consider, that fiber formation is a surface-energy minimization process, starting with the generation of colloidal particles and their linear assembly, and ending with structural evolution of the aggregates into mature fibers. We propose that aggregation drives conformational change and that a conformational change is not essential to initiate the aggregation process.”

References:
Xu S. Aggregation drives "misfolding" in protein amyloid fiber formation. Amyloid. 2007 Jun;14(2):119-31. Abstract

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