The amorphous aggregation of A?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?1-40 fibrils are observed at high contact angles.
Amorphous Aggregation of Amyloid Beta 1-40 Peptide in Confined Space
Albonetti;Cristiano;Liscio;Fabiola;Milita;Silvia;Fabio
2015
Abstract
The amorphous aggregation of A?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?1-40 fibrils are observed at high contact angles.File in questo prodotto:
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