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Direct Observation of Time-Resolved Polymorphic States in the Self-Assembly of End-Capped Heptapeptides



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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).

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