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Fibrillation processes in peptides: Structural states in the time-dependent self-assembly of an amyloid heptapeptide were resolved by single-molecule atomic force microscopy. Statistical analysis of the structures and their topological details revealed a continuous evolution of the polymorphs over time from the initial small spherical micelles into protofilaments, helical ribbons, and finally nanotube-like structures (see picture). Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
Adamčík et al. (Fri,) studied this question.