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Updated: Apr 4, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
Amorphous Aggregation of Amyloid Beta 1-40 Peptide in Confined Space
Giulia Foschi1, Cristiano Albonetti2, Fabiola Liscio3
1Scriba Nanotecnologie S. r. L., Via Corticella 183 -, 40128, Bologna, Italy.
Abstract:
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.
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