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

作者:Foschi Giulia; Albonetti Cristiano*; Liscio Fabiola; Milita Silvia; Greco Pierpaolo; Biscarini Fabio
来源:ChemPhysChem, 2015, 16(16): 3379-3384.
DOI:10.1002/cphc.201500602

摘要

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

  • 出版日期2015-11-16