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
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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