Heterogeneous primary nucleation determines Aβ42 fibrilstructure.

Aβ42 fibril structure depends strongly on the aggregation vessel, with glass vials/bottles and PEGylated polystyrene 96-well plates producing very different monomer folds within fibrils.

• Why it matters: Multiple Aβ42 fibril structures can arise from differing environments, but the specific role of nucleation—especially whether it is homogeneous or heterogeneous—was unclear.
• What they did: Monomeric amyloid beta peptide (Aβ42) was aggregated in identical solutions in glass vials/bottles versus PEGylated polystyrene 96-well plates, and the resulting fibril structures were compared.
• The result: The vessel-linked structural differences indicate extremely slow homogeneous primary nucleation and suggest heterogeneous primary nucleation at vessel walls or the air–water–wall three-line interface, with the initial structure then propagated by elongation and secondary nucleation.

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