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This article is part of the supplement: Proceedings of the 8th International Conference on Alzheimer's Disease Drug Discovery

Open Access Review

Preventing β-amyloid fibrillization and deposition: β-sheet breakers and pathological chaperone inhibitors

Thomas Wisniewski123* and Martin Sadowski124

Author affiliations

1 Department of Neurology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA

2 Department of Pathology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA

3 Department of Psychiatry, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA

4 Department of Pharmacology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA

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Citation and License

BMC Neuroscience 2008, 9(Suppl 2):S5  doi:10.1186/1471-2202-9-S2-S5

Published: 3 December 2008

Abstract

Central to the pathogenesis of Alzheimer's disease (AD) is the conversion of normal, soluble β-amyloid (sAβ) to oligomeric, fibrillar Aβ. This process of conformational conversion can be influenced by interactions with other proteins that can stabilize the disease-associated state; these proteins have been termed 'pathological chaperones'. In a number of AD models, intervention that block soluble Aβ aggregation, including β-sheet breakers, and compounds that block interactions with pathological chaperones, have been shown to be highly effective. When combined with early pathology detection, these therapeutic strategies hold great promise as effective and relatively toxicity free methods of preventing AD related pathology.