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Interactions between a luminescent conjugated oligoelectrolyte and insulin during early phases of amyloid formation
Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
Experimental Biomolecular Physics, Department of Applied Physics, Royal Institute of Technology, SE-106 91 Stockholm, Sweden.
Experimental Biomolecular Physics, Department of Applied Physics, Royal Institute of Technology, SE-106 91 Stockholm, Sweden.
Linköping University, Department of Physics, Chemistry and Biology, Biomolecular and Organic Electronics . Linköping University, The Institute of Technology.
2011 (English)In: Macromolecular Bioscience, ISSN 1616-5187, E-ISSN 1616-5195, Vol. 11, no 8, 1120-1127 p.Article in journal (Refereed) Published
Abstract [en]

Folding of an amino acid polypeptide chain into its native three-dimensional protein is a delicate process. Misfolding may cause assembly of dysfunctional proteins leading to aggregated assemblies, in medicine denoted amyloids, causing Alzheimer’s, Parkinson and a number of other protein related diseases. Amyloids have also shown promising results as building blocks in organic electronic applications, associated to conjugated polymers. Luminescent conjugated oligo- and polythiophenes (LCPs) have been further developed for biosensor applications exhibiting good ability to discriminate and determine different types of amyloid enrichment in complex environments, such as in tissue sections. The nature of interaction between the amyloid assemblies and LCPs is still not fully understood. In this study we use steady-state fluorescence spectroscopy, dynamic light scattering, transmission electron microscopy and fluorescence correlation spectroscopy to follow the interplay between the anionic oligothiophene derivative 4',3'''-Bis-carboxymethyl-[2,2';5',2'';5'',2''';5''',2'''']quinque thiophene-5,5''''-dicarboxylic acid (p-FTAA), and prefibrillar protein assemblies present during the earlier stage of in vitro fibrillation of bovine insulin. Our findings confirm that p-FTAA interacts with pre-fibrillar species of insulin preceding the formation of mature insulin amyloid fibrils, and insights regarding the molecular interplay between p-FTAA and these species are provided.

Place, publisher, year, edition, pages
Wiley , 2011. Vol. 11, no 8, 1120-1127 p.
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:liu:diva-54898DOI: 10.1002/mabi.201100016ISI: 000294160900011OAI: oai:DiVA.org:liu-54898DiVA: diva2:311086
Note
Funding Agencies|Swedish Science Council (VR)||Strategic Research Foundation (SSF) through the center for organic bioelectronics (OBOE)||Knut and Alice Wallenberg foundation||Available from: 2010-04-20 Created: 2010-04-20 Last updated: 2017-12-12
In thesis
1. Conjugated Polyelectrolytes in Interactions with Biomolecules for Supramolecular assembly and Sensing
Open this publication in new window or tab >>Conjugated Polyelectrolytes in Interactions with Biomolecules for Supramolecular assembly and Sensing
2010 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Conjugated polyelectrolytes (CP) show interesting electrical and optical properties for organic electronics as well as for life science applications. Their possibilities of supramolecular assembly with nanowire like misfolded proteins, amyloids, as well as synthetic polypeptides or DNA forming conducting or luminescent nano composites is highly interesting as being a truly bottom up approach for fabrication of OLEDs, photovoltaic’s as well as logic devices. The conformation and aggregation dependent luminescence properties from the special class of CPs, Luminescent conjugated polyelectrolytes (LCP), have been utilised and developed as sensors to follow and study biomolecular interactions, DNA hybridisation, protein-protein interactions and staining of living cell cultures and tissue slides. In this thesis we are bringing the evolution a few steps further by applying new types of experimental techniques, such as light scattering and fluorescence correlation spectroscopy, combined with standard techniques as soft lithography and different spectroscopy techniques, to gain better knowledge of the optical behaviour of LCPs and their interactions with biomolecules. We explore the optical properties and vibronic transitions of LCPs; their ability of resonance energy transfer with LCPs indicating super lightning behaviour; the opposite fluorescence shift when interacting with α-helical rich polypeptides compared to earlier reports of interactions upon staining of β-rich amyloids; and the possibility of LCPs to influence protein aggregation as well as the possibility of fabricating biochips based on LCPs and soft lithography. Here we also show fundamental limitations to patterning using macromolecular fluids, of general relevance to soft lithography and nanoimprint lithography with low viscosity polymers.

Place, publisher, year, edition, pages
Linköping: Linköping University Electronic Press, 2010. 60 p.
Series
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 1308
National Category
Natural Sciences
Identifiers
urn:nbn:se:liu:diva-54902 (URN)978-91-7393-408-4 (ISBN)
Public defence
2010-05-14, Planck, Fysikhuset, Campus Valla, Linköpings universitet, Linköping, 14:00 (English)
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Available from: 2010-04-20 Created: 2010-04-20 Last updated: 2014-04-08Bibliographically approved

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Wigenius, Jens A.Inganäs, Olle

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