Microfluidics reveals a flow-induced large scale polymorphism of protein aggregates

Vito Foderà; S Pagliara; O Otto; UF Keyser; AM Donald

Microfluidics reveals a flow-induced large scale polymorphism of protein aggregates

Vito Foderà, S Pagliara, O Otto, UF Keyser, AM Donald

33 Citationer (Scopus)

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.

Originalsprog	Engelsk
Tidsskrift	Journal of Physical Chemistry Letters
Vol/bind	3
Sider (fra-til)	2803-2807
ISSN	1948-7185
Status	Udgivet - 4 okt. 2012
Udgivet eksternt	Ja

Citationsformater

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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.",

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T1 - Microfluidics reveals a flow-induced large scale polymorphism of protein aggregates

AU - Foderà, Vito

AU - Pagliara, S

AU - Otto, O

AU - Keyser, UF

AU - Donald, AM

PY - 2012/10/4

Y1 - 2012/10/4

N2 - 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.

AB - 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.

M3 - Journal article

SN - 1948-7185

VL - 3

SP - 2803

EP - 2807

JO - Journal of Physical Chemistry Letters

JF - Journal of Physical Chemistry Letters

ER -

Microfluidics reveals a flow-induced large scale polymorphism of protein aggregates

Abstract

Fingeraftryk

Citationsformater