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A variety of thiophene based ligands for detection of protein aggregates by surface plasmon resonance
Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska fakulteten.
Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska fakulteten.
Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska fakulteten.
Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska fakulteten.
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(engelsk)Manuskript (preprint) (Annet vitenskapelig)
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.

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Identifikatorer
URN: urn:nbn:se:liu:diva-122274OAI: oai:DiVA.org:liu-122274DiVA, id: diva2:865141
Tilgjengelig fra: 2015-10-27 Laget: 2015-10-27 Sist oppdatert: 2015-10-27bibliografisk kontrollert
Inngår i avhandling
1. Asymmetric Oligothiophenes: Chemical Evolution of Multimodal Amyloid Ligands
Åpne denne publikasjonen i ny fane eller vindu >>Asymmetric Oligothiophenes: Chemical Evolution of Multimodal Amyloid Ligands
2015 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
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.

sted, utgiver, år, opplag, sider
Linköping: Linköping University Electronic Press, 2015. s. 67
Serie
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 1692
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Identifikatorer
urn:nbn:se:liu:diva-122278 (URN)10.3384/diss.diva-122278 (DOI)978-91-7685-987-2 (ISBN)
Disputas
2015-11-20, Planck, Fysikhuset, Campus Valla, Linköping, 10:15 (svensk)
Opponent
Veileder
Tilgjengelig fra: 2015-10-27 Laget: 2015-10-27 Sist oppdatert: 2019-11-15bibliografisk kontrollert

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