Anionic Oligothiophenes Compete for Binding of X-34 but not PIB to Recombinant Aβ Amyloid Fibrils and Alzheimer's Disease Brain-Derived Aβ

Marcus Bäck, Hanna Appelqvist, Harry LeVine, K. Peter R. Nilsson

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

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 languageEnglish
Pages (from-to)18335-18338
Number of pages4
JournalChemistry - A European Journal
Volume22
Issue number51
DOIs
StatePublished - Dec 19 2016

Bibliographical note

Publisher Copyright:
© 2016 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.

Keywords

  • Alzheimer's disease
  • amyloid ligands
  • fluorescence
  • luminescent conjugated oligothiophenes
  • proteins

ASJC Scopus subject areas

  • Catalysis
  • Organic Chemistry

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