Sökning: (L773:2296 2646)
> (2016) >
Nanoscale Structure...
Nanoscale Structure and Spectroscopic Probing of A beta 1-40 Fibril Bundle Formation
-
- Psonka-Antonczyk, Katarzyna M. (författare)
- Department of Physics, Norwegian University of Science and Technology NTNU, Trondheim, Norway
-
- Hammarström, Per (författare)
- Linköpings universitet,Kemi,Tekniska fakulteten
-
- Johansson, Leif (författare)
- Linköpings universitet,Tekniska fakulteten,Kemi
-
visa fler...
-
- Lindgren, Mikael (författare)
- Linköpings universitet,Kemi,Tekniska fakulteten,Department of Physics, Norwegian University of Science and Technology NTNU, Trondheim, Norway
-
- Stokke, Björn T. (författare)
- Department of Physics, Norwegian University of Science and Technology NTNU, Trondheim, Norway
-
- Nilsson, Peter (författare)
- Linköpings universitet,Kemi,Tekniska fakulteten
-
- Nyström, Sofie (författare)
- Linköpings universitet,Kemi,Tekniska fakulteten
-
visa färre...
-
(creator_code:org_t)
- 2016-11-22
- 2016
- Engelska.
-
Ingår i: Frontiers in Chemistry. - : Frontiers Research Foundation. - 2296-2646. ; 4
- Relaterad länk:
-
https://liu.diva-por... (primary) (Raw object)
-
visa fler...
-
https://www.frontier...
-
https://urn.kb.se/re...
-
https://doi.org/10.3...
-
visa färre...
Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Farmaceutiska vetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Pharmaceutical Sciences (hsv//eng)
Nyckelord
- amyloids
- amyloid formation
- AFM
- hyperspectral imaging
- SPR
- fibrillation
- oligothiophenes
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas