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Tuning the aqueous self-assembly process of insulin by a hydrophobic additive
Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics. Linköping University, Faculty of Science & Engineering.
2015 (English)In: RSC ADVANCES, ISSN 2046-2069, Vol. 5, no 112, 92254-92262 p.Article in journal (Refereed) Published
Abstract [en]

Biomolecular self-assembly is an efficient way of preparing soft-matter based materials. Herein we report a novel method, based on the use of insoluble additives in aqueous media, for influencing the self-assembly process. Due to their low solubility, the use of hydrophobic additives in aqueous media is problematic; however, by mixing the additive with the biomolecule in the solid state, prior to solvation, this problem can be circumvented. In the investigated self-assembly system, where bovine insulin self-assembles into spherical structures, the inclusion of the hydrophobic material α-sexithiophene (6T) results in significant changes in the self-assembly process. Under our reaction conditions, in the case of materials prepared from insulin-only the growth of spherulites typically stops at a diameter of 150μm. However, by adding 2 weight % of hydrophobic material, spherulite growth continues up to diameters in the mm-range. The spherulites incorporate 6T and are thus fluorescent. The method reported herein should be of interest to all scientists working in the field of self-assembly as the flexible materials preparation, based simply on co-grinding of commercially available materials, adds another option to influence the structure and properties of products formed by  self-assembly reactions.

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2015. Vol. 5, no 112, 92254-92262 p.
National Category
Organic Chemistry Biomaterials Science
URN: urn:nbn:se:liu:diva-121018DOI: 10.1039/c5ra16144dISI: 000364032500040OAI: diva2:850847

Funding agencies: Swedish Government Strategic Research Area in Materials Science on Functional Materials at Linkoping University (Faculty Grant SFO-Mat-LiU) [2009-00971]; Knut and Alice Wallenberg foundation

Available from: 2015-09-02 Created: 2015-09-02 Last updated: 2015-12-03
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, Fredrik G.Solin, Niclas
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