Abstract
Beta amyloid protein (Aβ) is one of the intrinsically disordered proteins associated with neurodegenerative diseases like Parkinson’s, prion disease and Alzheimer’s disease (AD) in particular. Although the direct involvement of Aβ peptides in AD is well documented and their aggregative ability is closely related to their neurotoxicity, the precise mechanism of the neurotoxic effects of Aβ peptides remains unclear. There is still a significant gap between the site-specific structural information and the complex structural diversity of Aβ amyloids. The description of the structural polymorphisms of Aβ amyloids can provide valuable information of the molecular basis of AD onset-progress and is essential for comprehension of the Aβ aggregation pathways, in particular its structural evolution. In this review we tried to illustrate the emerging trend of defining several human neurodegenerative disorders as syndromes of protein folding and oligomerization through the example of AD.
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- 1.
European Commission website 2014. Neurodegenerative Disorders. Accessed 26 October 2014. http://ec.europa.eu/health/major_chronic_diseases/diseases/brain_neurological/index_en.htm.
- 2.
Alzheimer’s Disease International website 2014. World Alzheimer’s Reports. Accessed 26 October 2014. http://www.alz.co.uk/research/world-report.
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Korsak, M., Kozyreva, T. (2015). Beta Amyloid Hallmarks: From Intrinsically Disordered Proteins to Alzheimer’s Disease. In: Felli, I., Pierattelli, R. (eds) Intrinsically Disordered Proteins Studied by NMR Spectroscopy. Advances in Experimental Medicine and Biology, vol 870. Springer, Cham. https://doi.org/10.1007/978-3-319-20164-1_14
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