Amorphous Aggregation of Amyloid Beta 1-40 Peptide in Confined Space

Giulia Foschi, Cristiano Albonetti, Fabiola Liscio, Silvia Milita, Pierpaolo Greco e Fabio Biscarini

ChemPhysChem 2015, 16(16), 3379-3384.


The amorphous aggregation of Aβ1-40 peptide is addressed by using micromolding in capillaries. Both the morphology and the size of the aggregates are modulated by changing the contact angle of the sub-micrometric channel walls. Upon decreasing the hydrophilicity of the channels, the aggregates change their morphology from small aligned drops to discontinuous lines, thereby keeping their amorphous structure. Aβ1-40 fibrils are observed at high contact angles.