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Amorphous Aggregation of Amyloid Beta 1‐40 Peptide in Confined Space
Author(s) -
Foschi Giulia,
Albonetti Cristiano,
Liscio Fabiola,
Milita Silvia,
Greco Pierpaolo,
Biscarini Fabio
Publication year - 2015
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201500602
Subject(s) - amorphous solid , morphology (biology) , contact angle , materials science , fibril , peptide , chemical engineering , crystallography , chemistry , nanotechnology , chemical physics , composite material , biochemistry , genetics , engineering , biology
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.