Super‐Resolution Infrared Imaging of Polymorphic Amyloid Aggregates Directly in Neurons
Klementieva, Oxana LU
; Sandt, Christophe
; Martinsson, Isak
LU
; Kansiz, Mustafa
; Keppler Gouras, Gunnar
LU
and Borondics, Ferenc
(2020)
In Advanced Science
- Abstract
- Loss of memory during Alzheimer's disease (AD), a fatal neurodegenerative disorder, is associated with neuronal loss and the aggregation of amyloid proteins into neurotoxic β‐sheet enriched structures. However, the mechanism of amyloid protein aggregation is still not well understood due to many challenges when studying the endogenous amyloid structures in neurons or in brain tissue. Available methods either require chemical processing of the sample or may affect the amyloid protein structure itself. Therefore, new approaches, which allow studying molecular structures directly in neurons, are urgently needed. A novel approach is tested, based on label‐free optical photothermal infrared super‐resolution microspectroscopy, to study... (More)
- Loss of memory during Alzheimer's disease (AD), a fatal neurodegenerative disorder, is associated with neuronal loss and the aggregation of amyloid proteins into neurotoxic β‐sheet enriched structures. However, the mechanism of amyloid protein aggregation is still not well understood due to many challenges when studying the endogenous amyloid structures in neurons or in brain tissue. Available methods either require chemical processing of the sample or may affect the amyloid protein structure itself. Therefore, new approaches, which allow studying molecular structures directly in neurons, are urgently needed. A novel approach is tested, based on label‐free optical photothermal infrared super‐resolution microspectroscopy, to study AD‐related amyloid protein aggregation directly in the neuron at sub‐micrometer resolution. Using this approach, amyloid protein aggregates are detected at the subcellular level, along the neurites and strikingly, in dendritic spines, which has not been possible until now. Here, a polymorphic nature of amyloid structures that exist in AD transgenic neurons is reported. Based on the findings of this work, it is suggested that structural polymorphism of amyloid proteins that occur already in neurons may trigger different mechanisms of AD progression. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/cf38fc99-2ab4-4293-a7f8-8f944c308d26
- author
- Klementieva, Oxana
LU
; Sandt, Christophe
; Martinsson, Isak
LU
; Kansiz, Mustafa
; Keppler Gouras, Gunnar
LU
and Borondics, Ferenc
- organization
- publishing date
- 2020-02-07
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Optical photothermal infrared spectroscopyon, Alzheimer’s disease, protein aggregation, structure-function relation, disease mechanism, super-resolution, Alzheimer’s disease, aggregation, structure-function
- in
- Advanced Science
- article number
- 1903004
- pages
- 9 pages
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:85079066140
- pmid:32195099
- ISSN
- 2198-3844
- DOI
- 10.1002/advs.201903004
- language
- English
- LU publication?
- yes
- id
- cf38fc99-2ab4-4293-a7f8-8f944c308d26
- date added to LUP
- 2020-02-07 17:14:09
- date last changed
- 2023-11-19 23:13:43
@article{cf38fc99-2ab4-4293-a7f8-8f944c308d26,
abstract = {{Loss of memory during Alzheimer's disease (AD), a fatal neurodegenerative disorder, is associated with neuronal loss and the aggregation of amyloid proteins into neurotoxic β‐sheet enriched structures. However, the mechanism of amyloid protein aggregation is still not well understood due to many challenges when studying the endogenous amyloid structures in neurons or in brain tissue. Available methods either require chemical processing of the sample or may affect the amyloid protein structure itself. Therefore, new approaches, which allow studying molecular structures directly in neurons, are urgently needed. A novel approach is tested, based on label‐free optical photothermal infrared super‐resolution microspectroscopy, to study AD‐related amyloid protein aggregation directly in the neuron at sub‐micrometer resolution. Using this approach, amyloid protein aggregates are detected at the subcellular level, along the neurites and strikingly, in dendritic spines, which has not been possible until now. Here, a polymorphic nature of amyloid structures that exist in AD transgenic neurons is reported. Based on the findings of this work, it is suggested that structural polymorphism of amyloid proteins that occur already in neurons may trigger different mechanisms of AD progression.}},
author = {{Klementieva, Oxana and Sandt, Christophe and Martinsson, Isak and Kansiz, Mustafa and Keppler Gouras, Gunnar and Borondics, Ferenc}},
issn = {{2198-3844}},
keywords = {{Optical photothermal infrared spectroscopyon, Alzheimer’s disease, protein aggregation, structure-function relation, disease mechanism; super-resolution; Alzheimer’s disease; aggregation; structure-function}},
language = {{eng}},
month = {{02}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Advanced Science}},
title = {{Super‐Resolution Infrared Imaging of Polymorphic Amyloid Aggregates Directly in Neurons}},
url = {{http://dx.doi.org/10.1002/advs.201903004}},
doi = {{10.1002/advs.201903004}},
year = {{2020}},
}