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Amyloid fibrils as dispersing agents for oligothiophenes: control of photophysical properties through nanoscale templating and flow induced fibril alignment
Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
Chalmers, Sweden.
Chalmers, Sweden .
Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
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2014 (English)In: Journal of Materials Chemistry C, ISSN 2050-7526, Vol. 2, no 37, 7811-7822 p.Article in journal (Refereed) Published
Abstract [en]

Herein we report that protein fibrils formed from aggregated proteins, so called amyloid fibrils, serve as an excellent dispersing agent for hydrophobic oligothiophenes such as alpha-sexithiophene (6T). Furthermore, the protein fibrils are capable of orienting 6T along the fibril long axis, as demonstrated by flow-aligned linear dichroism spectroscopy and polarized fluorescence microscopy. The materials are prepared by solid state mixing of 6T with a protein capable of self-assembly. This results in a water soluble composite material that upon heating in aqueous acid undergoes self-assembly into protein fibrils non-covalently functionalized with 6T, with a typical diameter of 5-10 nm and lengths in the micrometre range. The resulting aqueous fibril dispersions are a readily available source of oligothiophenes that can be processed from aqueous solvent, and we demonstrate the fabrication of macroscopic structures consisting of aligned 6T functionalized protein fibrils. Due to the fibril induced ordering of 6T these structures exhibit polarized light emission.

Place, publisher, year, edition, pages
Royal Society of Chemistry , 2014. Vol. 2, no 37, 7811-7822 p.
National Category
Biological Sciences
URN: urn:nbn:se:liu:diva-111311DOI: 10.1039/c4tc00692eISI: 000341458000013OAI: diva2:755254

Funding Agencies|Swedish Research Council [20114324]; Swedish Strategic Research Foundation (SSF); Knut and Alice Wallenberg foundation through a Wallenberg Scholar grant; Chalmers Area of Advance in Nanoscience and Nanotechnology; Swedish Government Strategic Research Area in Materials Science on Functional Materials at Linkoping University (Faculty Grant SFO-Mat-LiU) [2009-00971]

Available from: 2014-10-14 Created: 2014-10-14 Last updated: 2015-09-02
In thesis
1. Preparation and Application of Functionalized Protein Fibrils
Open this publication in new window or tab >>Preparation and Application of Functionalized Protein Fibrils
2015 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Many proteins have an innate ability to self-assemble into fibrous structures known as amyloid fibrils. From a material science perspective, fibrils have several interesting characteristics, including a high stability, a distinct shape and tunable surface properties. Such structures can be given additional properties through functionalization by other compounds such as fluorophores. Combination of fibrils with a function yielding compound can be achieved in several ways. Covalent bond attachment is specific, but cumbersome. External surface adhesion is nonspecific, but simple. However, in addition, internal non-covalent functionalization is possible. In this thesis, particular emphasis is put on internal functionalization of fibrils; by co-grinding fibril forming proteins with a hydrophobic molecule, a protein-hydrophobic compound molecule composite can be created that retains the proteins innate ability to form fibrils. Subsequently formed fibrils will thus have the structural properties of the protein fibril as well as the properties of the incorporated compound. The functionalization procedures used throughout this thesis are applicable for a wide range of chromophores commonly used for organic electronics and photonics. The methods developed and the prepared materials are useful for applications within optoelectronics as well as biomedicine.

Regardless of the methodology of functionalization, using functionalized fibrils in a controlled fashion for material design requires an intimate understanding of the formation process and knowledge of the tools available to control not only the formation but also any subsequent macroscale assembly of fibrils. The development and application of such tools are described in several of the papers included in this thesis. With the required knowledge in hand, the possible influence of fibrils on the functionalizing agents, and vice versa, can be probed. The characteristic traits of the functionalized fibril can be customized and the resulting material can be organized and steered towards a specific shape and form. This thesis describes how control over the process of formation, functionalization and organization of functionalized fibrils can be utilized to influence the hierarchical assembly of fibrils – ranging from spherical structures to  spirals; the function – fluorescent or conducting; and macroscopic properties – optical birefringence and specific arrangement of functionalized fibrils in the solid state. In conclusion, the use of amyloid fibrils in material science has great potential. Herein is presented a possible route towards a fully bottom up approach ranging from the nanoscale to the macroscale.

Place, publisher, year, edition, pages
Linköping: Linköping University Electronic Press, 2015. 70 p.
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 1695
National Category
Cell and Molecular Biology Physical Chemistry Physical Chemistry
urn:nbn:se:liu:diva-121022 (URN)978-91-7685-978-0 (print) (ISBN)
Public defence
2015-09-11, Planck, Fysikhuset, Campus Valla, Linköping, 10:15 (English)
Available from: 2015-09-02 Created: 2015-09-02 Last updated: 2015-09-02Bibliographically approved

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Bäcklund, FredrikInganäs, OlleSolin, Niclas
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