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An azide functionalized oligothiophene ligand - A versatile tool for multimodal detection of disease associated protein aggregates
Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska högskolan.
Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska högskolan.
Linköpings universitet, Institutionen för fysik, kemi och biologi, Teknisk biologi. Linköpings universitet, Tekniska högskolan.
Linköpings universitet, Institutionen för fysik, kemi och biologi, Kemi. Linköpings universitet, Tekniska högskolan.
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2015 (engelsk)Inngår i: Biosensors & bioelectronics, ISSN 0956-5663, E-ISSN 1873-4235, Vol. 63, s. 204-211Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Ligands for identifying protein aggregates are of great interest as such deposits are the pathological hallmark of a wide range of severe diseases including Alzheimers and Parkinsons disease. Here we report the synthesis of an azide functionalized fluorescent pentameric oligothiophene that can be utilized as a ligand for multimodal detection of disease-associated protein aggregates. The azide functionalization allows for attachment of the ligand to a surface by conventional click chemistry without disturbing selective interaction with protein aggregates and the oligothiophene-aggregate interaction can be detected by fluorescence or surface plasmon resonance. In addition, a methodology where the oligothiophene ligand is employed as a capturing molecule selective for aggregated proteins in combination with an antibody detecting a distinct peptide/protein is also presented. We foresee that this methodology will offer the possibility to create a variety of multiplex sensing systems for sensitive and selective detection of protein aggregates, the pathological hallmarks of several neurodegenerative diseases.

sted, utgiver, år, opplag, sider
Elsevier , 2015. Vol. 63, s. 204-211
Emneord [en]
Protein aggregates; Oligothiophene; Fluorescence; Surface plasmon resonance; Click chemistry
HSV kategori
Identifikatorer
URN: urn:nbn:se:liu:diva-112169DOI: 10.1016/j.bios.2014.07.042ISI: 000343337000030PubMedID: 25089818OAI: oai:DiVA.org:liu-112169DiVA, id: diva2:764291
Merknad

Funding Agencies|Swedish Foundation for Strategic Research; Ehrling Persson Foundation; ERC Starting Independent Researcher grant (Project: MUMID)

Tilgjengelig fra: 2014-11-18 Laget: 2014-11-18 Sist oppdatert: 2019-01-22
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
HSV kategori
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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