Abstract
Amyloid fibrils are characterized by a structural arrangement of cross β-sheet as a common motif. However they can also experience a more complicated packing into a variety of 3D supramolecular structures (polymorphism). Confinement and flow rate play a crucial role in protein aggregation in living systems, but controlling such parameters during in vitro experiments still remains an unsolved problem. Here we present evidence of the effect of flow rate on the aggregation process in a confined environment using microfluidics. Specifically, we show that a gradual transition from spherical aggregates, that is, spherulites, to thick fiber-like structures takes place as a result of increasing the flow rate. Such results have implications both for a basic understanding of the mechanism behind aggregation phenomena and in the development of novel biomaterials.
| Original language | English |
|---|---|
| Journal | Journal of Physical Chemistry Letters |
| Volume | 3 |
| Pages (from-to) | 2803-2807 |
| ISSN | 1948-7185 |
| Publication status | Published - 4 Oct 2012 |
| Externally published | Yes |