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.

Amorphous Aggregation of Amyloid Beta 1-40 Peptide in Confined Space / Foschi, Giulia; Albonetti, Cristiano; Liscio, Fabiola; Milita, Silvia; Greco, Pierpaolo; Biscarini, Fabio. - In: CHEMPHYSCHEM. - ISSN 1439-4235. - ELETTRONICO. - 16:16(2015), pp. 3379-3384. [10.1002/cphc.201500602]

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

FOSCHI, GIULIA;Greco, Pierpaolo;BISCARINI, FABIO
2015

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.
14-set-2015
16
16
3379
3384
Amorphous Aggregation of Amyloid Beta 1-40 Peptide in Confined Space / Foschi, Giulia; Albonetti, Cristiano; Liscio, Fabiola; Milita, Silvia; Greco, Pierpaolo; Biscarini, Fabio. - In: CHEMPHYSCHEM. - ISSN 1439-4235. - ELETTRONICO. - 16:16(2015), pp. 3379-3384. [10.1002/cphc.201500602]
Foschi, Giulia; Albonetti, Cristiano; Liscio, Fabiola; Milita, Silvia; Greco, Pierpaolo; Biscarini, Fabio
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11380/1081862
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