Abstract
Alzheimer's disease and cerebral amyloid angiopathy are characterized by the deposition of β-amyloid fibrils consisting of 40- and 42-mer peptides (Aβ40 and Aβ42). Since the aggregation (fibrilization) of these peptides is closely related to the pathogenesis of these diseases, numerous structural analyses of Aβ40 and Aβ42 fibrils have been carried out. Aβ42 plays a more important role in the pathogenesis of these diseases since its aggregative ability and neurotoxicity are considerably greater than those of Aβ40. This review summarizes mainly our own recent findings from the structural analysis of Aβ42 fibrils and discusses its relevance to their neurotoxicity in vitro.
Original language | English |
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Pages (from-to) | 437-447 |
Number of pages | 11 |
Journal | Journal of Bioscience and Bioengineering |
Volume | 99 |
Issue number | 5 |
DOIs | |
Publication status | Published - 2005 May |
Keywords
- Alzheimer's disease
- Amyloid
- Aβ40
- Aβ42
- Cerebral amyloid angiopathy
- Familial Alzheimer's disease
- Neurotoxicity
- Oxidative stress
- Solid-state nuclear magnetic resonance
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology