Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9603213 | Journal of Bioscience and Bioengineering | 2005 | 11 Pages |
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.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Kazuhiro Irie, Kazuma Murakami, Yuichi Masuda, Akira Morimoto, Hajime Ohigashi, Ryutaro Ohashi, Kiyonori Takegoshi, Masaya Nagao, Takahiko Shimizu, Takuji Shirasawa,