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Morphology-Specific Inhibition of β-Amyloid Aggregates by 17β-Hydroxysteroid Dehydrogenase Type 10

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Author(s)

  • Laura Aitken
  • Steven D. Quinn
  • Cibran Perez-Gonzalez
  • Ifor D. W. Samuel
  • J. Carlos Penedo
  • Frank J. Gunn-Moore

Department/unit(s)

Publication details

JournalChembiochem
DateE-pub ahead of print - 16 Mar 2016
DatePublished (current) - 2 Jun 2016
Issue number11
Volume17
Number of pages9
Pages (from-to)1029-1037
Early online date16/03/16
Original languageEnglish

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.

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© 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

    Research areas

  • Alzheimer's disease, amyloid beta-peptides, dehydrogenases, fluorescent probes, neurochemistry

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