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

Authors
Journal
BMC Neuroscience
1471-2202
Publisher
Springer (Biomed Central Ltd.)
Publication Date
Volume
9
Identifiers
DOI: 10.1186/1471-2202-9-s2-s5
Keywords
  • Review
Disciplines
  • Biology
  • Medicine

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.

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