Amorphous Aggregation of Amyloid Beta 1‐40 Peptide in Confined Space. Issue 16 (14th September 2015)

• Record Type: Journal Article
• Authors: Foschi, Giulia; Albonetti, Cristiano; Liscio, Fabiola; Milita, Silvia; Greco, Pierpaolo; Biscarini, Fabio
• Is Part Of: Chemphyschem. Volume 16:Issue 16(2015)
• Page Start: 3379
• Page End: 3384
• Publication Date: 2015-09-14
• Subjects: Alzheimer's disease -- amyloid -- biotechnology -- nanotechnology -- scanning probe microscopy; Chemistry, Physical and theoretical -- Periodicals; 541.05
• DOI: 10.1002/cphc.201500602
• Languages: English
• ISSNs: 1439-4235

Abstract

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. 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.