Aitken, Laura, Quinn, Steven D. orcid.org/0000-0003-3442-4103, Perez-Gonzalez, Cibran et al. (3 more authors) (2016) Morphology-Specific Inhibition of β-Amyloid Aggregates by 17β-Hydroxysteroid Dehydrogenase Type 10. Chembiochem. pp. 1029-1037. ISSN 1439-7633
Abstract
A major hallmark of Alzheimer's disease (AD) is the formation of toxic aggregates of the β-amyloid peptide (Aβ). Given that Aβ peptides are known to localise within mitochondria and interact with 17β-HSD10, a mitochondrial protein expressed at high levels in AD brains, we investigated the inhibitory potential of 17β-HSD10 against Aβ aggregation under a range of physiological conditions. Fluorescence self-quenching (FSQ) of Aβ(1-42) labelled with HiLyte Fluor 555 was used to evaluate the inhibitory effect under conditions established to grow distinct Aβ morphologies. 17β-HSD10 preferentially inhibits the formation of globular and fibrillar-like structures but has no effect on the growth of amorphous plaque-like aggregates at endosomal pH 6. This work provides insights into the dependence of the Aβ-17β-HSD10 interaction with the morphology of Aβ aggregates and how this impacts enzymatic function. 17 β-HSD10 interaction with Aβ amyloid: what type of amyloid? 17β-hydroxysteroid dehydrogenase type 10 interacts with β-amyloid (Aβ) aggregates and suppresses Aβ-induced apoptosis in neurons, but the aggregate morphology inhibited by 17β-HSD10 remains unknown. Fluorescence self-quenching demonstrated that fibrils and globular aggregates, but not plaques, are targeted by 17β-HSD10.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details |
Keywords: | Alzheimer's disease,amyloid beta-peptides,dehydrogenases,fluorescent probes,neurochemistry |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Physics (York) The University of York > Faculty of Sciences (York) > Biology (York) |
Depositing User: | Pure (York) |
Date Deposited: | 21 Jun 2018 13:50 |
Last Modified: | 07 Feb 2025 00:21 |
Published Version: | https://doi.org/10.1002/cbic.201600081 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1002/cbic.201600081 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:132435 |
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