Maturation of amyloid β fibrils alters their molecular stability-Reference-Cited by-同舟云学术

Maturation of amyloid β fibrils alters their molecular stability

Published:2023 Issue:22 Volume:25 Page:15099-15103
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Becker Stefan¹,Giller Karin¹,Sieme Daniel¹,Rezaei-Ghaleh Nasrollah²³^ORCID

Affiliation:

1. Department of NMR-based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, D-37077 Göttingen, Germany

2. Institute of Physical Biology, Heinrich Heine University Düsseldorf, Universitätsstraße 1, D-40225 Düsseldorf, Germany

3. Institute of Biological Information Processing, IBI-7: Structural Biochemistry, Forschungszentrum Jülich, D-52428 Jülich, Germany

Abstract

High-pressure NMR investigation of freshly prepared and aged amyloid-beta aggregates reveals that their stability against pressure-induced monomer dissociation is increased through maturation.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CP/D3CP01276J

Reference29 articles.

1. Alzheimer’s Disease: Epidemiology and Clinical Progression

2. The neuropathological diagnosis of Alzheimer’s disease

3. Prion-like features of misfolded Aβ and tau aggregates

4. Self-propagation of pathogenic protein aggregates in neurodegenerative diseases

5. Phases of Aβ-deposition in the human brain and its relevance for the development of AD

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