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Imaging distinct conformational states of amyloid-β fibrils in Alzheimer's disease using novel luminescent probes
Linköpings universitet, Institutionen för fysik, kemi och biologi, Organisk Kemi. Linköpings universitet, Tekniska högskolan.ORCID-id: 0000-0002-5582-140X
Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Organisk Kemi.
Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi.ORCID-id: 0000-0002-4303-4783
Vise andre og tillknytning
2007 (engelsk)Inngår i: ACS Chemical Biology, ISSN 1554-8929, Vol. 2, nr 8, s. 553-560Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Using luminescent conjugated polyelectrolyte probes (LCPs), we demonstrate the possibility to distinguish amyloid-β 1-42 peptide (Aβ1-42) fibril conformations, by analyzing in vitro generated amyloid fibrils of Aβ1-42 formed under quiescent and agitated conditions. LCPs were then shown to resolve such conformational heterogeneity of amyloid deposits in vivo. A diversity of amyloid deposits depending upon morphology and anatomic location was illustrated with LCPs in frozen ex vivo brain sections from a transgenic mouse model (tg-APPswe) of Alzheimer's disease. Comparative LCP fluorescence showed that compact-core plaques of amyloid β precursor protein transgenic mice were composed of rigid dense amyloid. A more abundant form of amyloid plaque displayed morphology of a compact center with a protruding diffuse exterior. Surprisingly, the compact center of these plaques showed disordered conformations of the fibrils, and the exterior was composed of rigid amyloid protruding from the disordered center. This type of plaque appears to grow from more loosely assembled regions toward solidified amyloid tentacles. This work demonstrates how application of LCPs can prove helpful to monitor aggregate structure of in vivo formed amyloid deposits such as architecture, maturity, and origin.

sted, utgiver, år, opplag, sider
2007. Vol. 2, nr 8, s. 553-560
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Identifikatorer
URN: urn:nbn:se:liu:diva-40622DOI: 10.1021/cb700116uLokal ID: 53662OAI: oai:DiVA.org:liu-40622DiVA, id: diva2:261471
Tilgjengelig fra: 2009-10-10 Laget: 2009-10-10 Sist oppdatert: 2019-11-08
Inngår i avhandling
1. Designing thiophene-based fluorescent probes for the study of neurodegenerative protein aggregation diseases: From test tube to in vivo experiments
Åpne denne publikasjonen i ny fane eller vindu >>Designing thiophene-based fluorescent probes for the study of neurodegenerative protein aggregation diseases: From test tube to in vivo experiments
2009 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Protein aggregation is an event related to numerous neurodegenerative diseases, such as Alzhemier’s disease and prion diseases. However little is known as to how and why the aggregates form and furthermore, the toxic specie may not be the mature fibril but an on route or off route specie towards mature aggregates. During this project molecular probes were synthesized that may shed some light to these questions. The probes are thiophene based and the technique used for detection was mainly fluorescence. It was shown that the previously established thiophene based in vitro staining technique is valid ex vivo and in vivo. This would not have been possible without the synthesis of a variety of functionalized polymeric thiophene based probes; their in vitro and ex vivo staining properties were taken into consideration when the design of the small oligomeric probes were decided upon. These probes were shown to spectrally distinguish different types of amyloid, pass the bloodbrain barrier within minutes and specifically and selectively stain protein aggregates in the brains of mice.

sted, utgiver, år, opplag, sider
Linköping: Linköping University Electronic Press, 2009. s. 68
Serie
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 1286
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-51731 (URN)978-91-7393-496-1 (ISBN)
Disputas
2009-12-17, Planck, Fysikhuset, Campus Valla, Linköpings universitet, Linköping, 13:15 (engelsk)
Opponent
Veileder
Tilgjengelig fra: 2009-11-16 Laget: 2009-11-16 Sist oppdatert: 2020-02-19bibliografisk kontrollert

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