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Nanoscale Structure and Spectroscopic Probing of A beta 1-40 Fibril Bundle Formation
Department of Physics, Norwegian University of Science and Technology NTNU, Trondheim, Norway.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.ORCID iD: 0000-0001-5827-3587
Linköping University, Department of Physics, Chemistry and Biology. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering. Department of Physics, Norwegian University of Science and Technology NTNU, Trondheim, Norway.
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2016 (English)In: Frontiers in Chemistry, E-ISSN 2296-2646, Vol. 4, article id 44Article in journal (Refereed) Published
Abstract [en]

Amyloid plaques composed of fibrillar Amyloid-beta (A beta) are hallmarks of Alzheimers disease. However, A beta fibrils are morphologically heterogeneous. Conformation sensitive luminescent conjugated oligothiophenes (LCOs) are versatile tools for monitoring such fibril polymorphism in vivo and in vitro. Biophysical methods applied on in vitro generated A beta fibrils, stained with LCOs with different binding and fluorescence properties, can be used to characterize the A beta fibrillation in depth, far beyond that possible for in vivo generated amyloid plaques. In this study, in vitro fibrillation of the A beta 1-40 peptide was monitored by time-lapse transmission electron microscopy, LCO fluorescence, and atomic force microscopy. Differences in the LCO binding in combination with nanoscale imaging revealed that spectral variation correlated with fibrils transforming from solitary filaments (empty set similar to 2.5 nm) into higher order bundled structures (empty set similar to 5 nm). These detailed in vitro experiments can be used to derive data that reflects the heterogeneity of in vivo generated A beta plaques observed by LCO fluorescence. Our work provides new structural basis for targeted drug design and molecular probe development for amyloid imaging.

Place, publisher, year, edition, pages
Frontiers Research Foundation , 2016. Vol. 4, article id 44
Keywords [en]
amyloids, amyloid formation, AFM, hyperspectral imaging, SPR, fibrillation, oligothiophenes
National Category
Pharmaceutical Sciences
Identifiers
URN: urn:nbn:se:liu:diva-133108DOI: 10.3389/fchem.2016.00044ISI: 000388126300001OAI: oai:DiVA.org:liu-133108DiVA, id: diva2:1055295
Note

Funding Agencies|Norwegian Research Council [183338/S10]; Swedish Alzheimer Foundation [AF-555511]; Goran Gustafsson Foundation; Swedish Research Council [2015-04521]; Swedish Brain Foundation; Swedish Foundation for Strategic Research

Available from: 2016-12-12 Created: 2016-12-09 Last updated: 2018-04-25Bibliographically approved

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Hammarström, PerJohansson, LeifLindgren, MikaelNilsson, PeterNyström, Sofie
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