Vadukul, Devkee M, Gbajumo, Oyinkansola, Marshall, Karen E and Serpell, Louise C (2017) Amyloidogenicity and toxicity of the reverse and scrambled variants of amyloid-β 1-42. FEBS Letters, 591 (5). pp. 822-830. ISSN 0014-5793
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Abstract
β-amyloid 1-42 (Aβ1-42) is a self-assembling peptide that goes through many conformational and morphological changes before forming the fibrils that are deposited in extracellular plaques characteristic of Alzheimer's disease. The link between Aβ1-42 structure and toxicity is of major interest, in particular, the neurotoxic potential of oligomeric species. Many studies utilise reversed (Aβ42-1) and scrambled (AβS) forms of amyloid-β as control peptides. Here, using circular dichroism, thioflavin T fluorescence and transmission electron microscopy, we reveal that both control peptides self-assemble to form fibres within 24 h. However, oligomeric Aβ reduces cell survival of hippocampal neurons, while Aβ42-1 and Aβs have reduced effect on cellular health, which may arise from their ability to assemble rapidly to form protofibrils and fibrils.
Item Type: | Article |
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Schools and Departments: | School of Life Sciences > Biochemistry |
Research Centres and Groups: | Dementia Research Group |
Depositing User: | Louise Serpell |
Date Deposited: | 04 Apr 2017 10:08 |
Last Modified: | 04 Apr 2017 10:27 |
URI: | http://srodev.sussex.ac.uk/id/eprint/67256 |
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