Sökning: onr:"swepub:oai:DiVA.org:liu-180291" >
The Luminescent Con...
The Luminescent Conjugated Oligothiophene h-FTAA Attenuates the Toxicity of Different A beta Species
-
- Sandin, Linnea (författare)
- Linköpings universitet,Avdelningen för neurobiologi,Medicinska fakulteten,Region Östergötland, Klinisk patologi
-
- Sjödin, Simon (författare)
- Linköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten
-
- Brorsson, Ann-Christin (författare)
- Linköpings universitet,Kemi,Tekniska fakulteten
-
visa fler...
-
- Kågedal, Katarina (författare)
- Linköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten
-
- Civitelli, Livia (författare)
- Linköpings universitet,Medicinska fakulteten,Avdelningen för cellbiologi,Univ Oxford, England
-
visa färre...
-
(creator_code:org_t)
- 2021-09-01
- 2021
- Engelska.
-
Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 60:37, s. 2773-2780
- Relaterad länk:
-
https://liu.diva-por... (primary) (Raw object)
-
visa fler...
-
https://pubs.acs.org...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas