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Anionic Oligothiophenes Compete for Binding of X-34 but not PIB to Recombinant A beta Amyloid Fibrils and Alzheimers Disease Brain-Derived A beta
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- Bäck, Marcus (author)
- Linköpings universitet,Kemi,Tekniska fakulteten
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- Appelqvist, Hanna (author)
- Linköpings universitet,Kemi,Tekniska fakulteten
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- LeVine, Harry III (author)
- University of Kentucky, KY 40536 USA
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- (creator_code:org_t)
- 2016-11-03
- 2016
- English.
- In: CHEMISTRY-A EUROPEAN JOURNAL. - : WILEY-V C H VERLAG GMBH. - 0947-6539. ; 22:51, s. 18335-18338
- Journal article (peer-reviewed)
Abstract
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- Deposits comprised of amyloid- (A) are one of the pathological hallmarks of Alzheimers 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 compoundB (PIB) from recombinant A amyloid fibrils and Alzheimers disease brain-derived A. Overall, we foresee that the oligothiophene scaffold offers the possibility to develop novel high-affinity ligands for A pathology only found in human AD brain, targeting a different site than PIB.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Farmaceutiska vetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Pharmaceutical Sciences (hsv//eng)
Keyword
- Alzheimers disease; amyloid ligands; fluorescence; luminescent conjugated oligothiophenes; proteins
Publication and Content Type
- ref (subject category)
- art (subject category)
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