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The Luminescent Con...
The Luminescent Conjugated Oligothiophene h-FTAA Attenuates the Toxicity of Different A beta Species
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- Sandin, Linnea (author)
- Linköpings universitet,Avdelningen för neurobiologi,Medicinska fakulteten,Region Östergötland, Klinisk patologi
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- Sjödin, Simon (author)
- Linköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten
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- Brorsson, Ann-Christin (author)
- Linköpings universitet,Kemi,Tekniska fakulteten
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- Kågedal, Katarina (author)
- Linköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten
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- Civitelli, Livia (author)
- Linköpings universitet,Medicinska fakulteten,Avdelningen för cellbiologi,Univ Oxford, England
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(creator_code:org_t)
- 2021-09-01
- 2021
- English.
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In: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 60:37, s. 2773-2780
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Abstract
Subject headings
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- The prevailing opinion is that prefibrillar beta-amyloid (A beta) species, rather than end-stage amyloid fibrils, cause neuronal dysfunction in Alzheimers disease, although the mechanisms behind A beta neurotoxicity remain to be elucidated. Luminescent conjugated oligothiophenes (LCOs) exhibit spectral properties upon binding to amyloid proteins and have previously been reported to change the toxicity of A beta(1- 42) and prion protein. In a previous study, we showed that an LCO, pentamer formyl thiophene acetic acid (p-FTAA), changed the toxicity of A beta(1-42). Here we investigated whether an LCO, heptamer formyl thiophene acetic acid (h-FTAA), could change the toxicity of A beta(1-42) by comparing its behavior with that of p-FTAA. Moreover, we investigated the effects on toxicity when A ss with the Arctic mutation (A beta Arc) was aggregated with both LCOs. Cell viability assays on SH-SY5Y neuroblastoma cells demonstrated that h-FTAA has a stronger impact on A beta(1-42) toxicity than does p-FTAA. Interestingly, h-FTAA, but not p-FTAA, rescued the A beta(Arc)-mediated toxicity. Aggregation kinetics and binding assay experiments with A beta(1-42) and A beta(Arc) when aggregated with both LCOs showed that h-FTAA and p-FTAA either interact with different species or affect the aggregation in different ways. In conclusion, h-FTAA protects against A beta(1-42) and A beta(Arc) toxicity, thus showing h-FTAA to be a useful tool for improving our understanding of the process of A beta aggregation linked to cytotoxicity.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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