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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.Several neurodegenerative diseases are classified as proteinopathies as they are associated with the aggregation of misfolded proteins.[1–3] Among them, Alzheimer’s (AD), Huntington’s, Parkinson’s and Prion diseases are hallmarked by fibrillar aggregates of misfolded amyloidogenic proteins (plaques) because of the overabundant amount accumulated in specific regions of the patient’s brain. Amyloid beta (Aβ) peptide aggregates and accumulates in two types of plaques: diffuse, that is, soluble non-amyloidogenic amorphous aggregates, and compact, that is, insoluble amyloidogenic fibrils.[4–5] The insolubility of plaques is one of the neurotoxicity distinctive features, so compact plaques are regarded as neurotoxic whereas diffuse ones are not.[6–7]
Publication date: 
1 Nov 2015

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

Biblio References: 
Volume: 16 Issue: 16 Pages: 3379-3384