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

The amorphous aggregation of A?1-40 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. A?1-40 fibrils are observed at high contact angles.