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Development and Application of Methodology for Rapid Screening of Potential Amyloid Probes
Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, The Institute of Technology.
2014 (English)In: ACS COMBINATORIAL SCIENCE, ISSN 2156-8952, Vol. 16, no 12, 721-729 p.Article in journal (Refereed) Published
Abstract [en]

Herein, we demonstrate that it is possible to rapidly screen hydrophobic fluorescent aromatic molecules with regards to their properties as amyloid probes. By grinding the hydrophobic molecule with the amyloidogenic protein insulin, we obtained a water-soluble composite material. When this material is dissolved and exposed to conditions promoting amyloid formation, the protein aggregates into amyloid fibrils incorporating the hydrophobic molecule. As a result, changes in the fluorescence spectra of the hydrophobic molecule can be correlated to the formation of amyloid fibrils, and the suitability of the hydrophobic molecular skeleton as an amyloid probe can thus be assessed. As a result, we discovered two new amyloid probes, of which one is the well-known laser dye DCM. The grinding method can also be used for rapid preparation of novel composite materials between dyes and proteins, which can be used in materials science applications such as organic electronics and photonics.

Place, publisher, year, edition, pages
ACS Publications , 2014. Vol. 16, no 12, 721-729 p.
Keyword [en]
amyloid probes; rapid screening; fluorescent; aromatic molecules; laser dye DCM
National Category
Biological Sciences
URN: urn:nbn:se:liu:diva-113169DOI: 10.1021/co5001212ISI: 000346114600009PubMedID: 25383488OAI: diva2:780349

Funding Agencies|Swedish Government Strategic Research Area in Materials Science on Functional Materials at Linkoping University [2009-00971]; Knut and Alice Wallenberg Foundation

Available from: 2015-01-14 Created: 2015-01-12 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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