Abstract
Deposits comprised of amyloid-β (Aβ) are one of the pathological hallmarks of Alzheimer's disease (AD) and small hydrophobic ligands targeting these aggregated species are used clinically for the diagnosis of AD. Herein, we observed that anionic oligothiophenes efficiently displaced X-34, a Congo Red analogue, but not Pittsburgh compound B (PIB) from recombinant Aβ amyloid fibrils and Alzheimer's disease brain-derived Aβ. Overall, we foresee that the oligothiophene scaffold offers the possibility to develop novel high-affinity ligands for Aβ pathology only found in human AD brain, targeting a different site than PIB.
| Original language | English |
|---|---|
| Pages (from-to) | 18335-18338 |
| Number of pages | 4 |
| Journal | Chemistry - A European Journal |
| Volume | 22 |
| Issue number | 51 |
| DOIs | |
| State | Published - Dec 19 2016 |
Bibliographical note
Publisher Copyright:© 2016 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.
Funding
| Funders | Funder number |
|---|---|
| Institute of Neurological Disorders and Stroke National Advisory Neurological Disorders and Stroke Council | R21NS080576 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- Alzheimer's disease
- amyloid ligands
- fluorescence
- luminescent conjugated oligothiophenes
- proteins
ASJC Scopus subject areas
- Catalysis
- General Chemistry
- Organic Chemistry
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