liu.seSearch for publications in DiVA
Change search
ReferencesLink to record
Permanent link

Direct link
A variety of thiophene based ligands for detection of protein aggregates by surface plasmon resonance
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
Show others and affiliations
(English)Manuscript (preprint) (Other academic)
Abstract [en]

By attaching an azide functional group via a tetraethylene glycol linker to the α-terminal position of a variety of oligothiophenes, thiophene-based ligands that can be utilized for detection of protein aggregates with surface plasmon resonance have been developed. All ligands displayed selectivity towards recombinant amyloid fibrils and the LCO/protein aggregate interaction could be detected by fluorescence as well as by surface plasmon resonance.

National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:liu:diva-122274OAI: oai:DiVA.org:liu-122274DiVA: diva2:865141
Available from: 2015-10-27 Created: 2015-10-27 Last updated: 2015-10-27Bibliographically approved
In thesis
1. Asymmetric Oligothiophenes: Chemical Evolution of Multimodal Amyloid Ligands
Open this publication in new window or tab >>Asymmetric Oligothiophenes: Chemical Evolution of Multimodal Amyloid Ligands
2015 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Luminescent conjugated polymers (LCPs) and luminescent conjugated oligothiophenes (LCOs) can be used as molecular probes to study diseases associated with protein aggregation. The conventionally used dyes to study and detect protein aggregates, denoted amyloid, have been Congo red (CR) and Thioflavin T (ThT). In contrast to these amyloid ligands, LCOs offer the possibility to detect aggregated proteinaceous species occurring at earlier stages of amyloid formation as well as to distinguish different morphotypes of protein aggregates. The interaction between the LCOs and the protein deposits can be studied by fluorescence spectroscopy and microscopy both in vitro and ex vivo. In this thesis we report the development of multimodal asymmetric LCOs that can be utilized with two novel techniques, Surface Plasmon Resonance (SPR) and Positron Emission Tomography (PET), to study the interaction between LCO and amyloid fibrils in real time. With SPR, we have been able to determine binding affinities between LCO and amyloid, and with PET we have shown that radiolabelled LCOs can be used as a non-invasive method to study amyloid deposits in vivo. In addition, by alteration of the backbone (change of thiophene units), and of adding different side chains functionalities, we have shown that the properties of the amyloid ligands have a huge impact of the binding to different stages or forms of protein aggregates. By making asymmetrical LCOs, which can be attached to a surface, we also foresee a methodology that will offer the possibility to create a sensitive and selective detection method, and maybe lead to a lab-on-a-chip-application.

Place, publisher, year, edition, pages
Linköping: Linköping University Electronic Press, 2015. 67 p.
Series
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 1692
National Category
Chemical Sciences
Identifiers
urn:nbn:se:liu:diva-122278 (URN)10.3384/diss.diva-122278 (DOI)978-91-7685-987-2 (print) (ISBN)
Public defence
2015-11-20, Planck, Fysikhuset, Campus Valla, Linköping, 10:15 (Swedish)
Opponent
Supervisors
Available from: 2015-10-27 Created: 2015-10-27 Last updated: 2015-11-02Bibliographically approved

Open Access in DiVA

No full text

Search in DiVA

By author/editor
Johansson, Leif B. G.Bäck, MarcusLantz, LindaEriksson, MikaelaNygren, PatrikNilsson, Peter R.
By organisation
ChemistryFaculty of Science & Engineering
Chemical Sciences

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Total: 68 hits
ReferencesLink to record
Permanent link

Direct link