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Continuous Isotropic-Nematic Transition in Amyloid Fibril Suspensions Driven by Thermophoresis.


ABSTRACT: The isotropic and nematic (I?+?N) coexistence for rod-like colloids is a signature of the first-order thermodynamics nature of this phase transition. However, in the case of amyloid fibrils, the biphasic region is too small to be experimentally detected, due to their extremely high aspect ratio. Herein, we study the thermophoretic behaviour of fluorescently labelled ?-lactoglobulin amyloid fibrils by inducing a temperature gradient across a microfluidic channel. We discover that fibrils accumulate towards the hot side of the channel at the temperature range studied, thus presenting a negative Soret coefficient. By exploiting this thermophoretic behaviour, we show that it becomes possible to induce a continuous I-N transition with the I and N phases at the extremities of the channel, starting from an initially single N phase, by generating an appropriate concentration gradient along the width of the microchannel. Accordingly, we introduce a new methodology to control liquid crystal phase transitions in anisotropic colloidal suspensions. Because the induced order-order transitions are achieved under stationary conditions, this may have important implications in both applied colloidal science, such as in separation and fractionation of colloids, as well as in fundamental soft condensed matter, by widening the accessibility of target regions in the phase diagrams.

SUBMITTER: Vigolo D 

PROVIDER: S-EPMC5430637 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature

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Continuous Isotropic-Nematic Transition in Amyloid Fibril Suspensions Driven by Thermophoresis.

Vigolo Daniele D   Zhao Jianguo J   Handschin Stephan S   Cao Xiaobao X   deMello Andrew J AJ   Mezzenga Raffaele R  

Scientific reports 20170427 1


The isotropic and nematic (I + N) coexistence for rod-like colloids is a signature of the first-order thermodynamics nature of this phase transition. However, in the case of amyloid fibrils, the biphasic region is too small to be experimentally detected, due to their extremely high aspect ratio. Herein, we study the thermophoretic behaviour of fluorescently labelled β-lactoglobulin amyloid fibrils by inducing a temperature gradient across a microfluidic channel. We discover that fibrils accumula  ...[more]

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