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Alzheimer's Society comment on new research into the toxicity of amyloid fibrils

Published 4 December 2009

A new study published today in the Journal of Biological Chemistry adds to our understanding of the toxicity of amyloid plaques – one of the protein deposits associated with Alzheimer's disease.

The research (published Friday 4 December 2009) studied small fibrils which make up amyloid plaques and found that the shorter the fibril the more toxic it becomes. For many years it has been believed that plaques are toxic, but recently research has focused on the toxicity of intermediary, smaller formations of the protein that have not yet assembled into fibrils or plaques.

Alzheimer's Society comment

'Amyloid may have more than one type of toxic effect depending on the level of its build up and shape. Some potential treatments for Alzheimer's disease centre around breaking up the amyloid plaques, so it is important to understand whether this process would generate more toxic material in the brain rather than less.

'These findings are a valuable step in understanding why nerve cells die in the presence of amyloid and could contribute to research into finding better treatments to prevent nerve cell death. Dementia research is desperately underfunded but with the right investment it can be defeated.'

Dr Susanne Sorensen
Head of Research
Alzheimer's Society

Ref Radford et al. 'Fibril fragmentation enhances amyloid cytotoxivity' Journal of Biological Chemistry, Dec 2009.