Structure of beta-amyloid fibrils and its relevance to their neurotoxicity: implications for the pathogenesis of Alzheimer's disease |
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Authors: | Irie Kazuhiro Murakami Kazuma Masuda Yuichi Morimoto Akira Ohigashi Hajime Ohashi Ryutaro Takegoshi Kiyonori Nagao Masaya Shimizu Takahiko Shirasawa Takuji |
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Affiliation: | Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto 606-8502, Japan. irie@kais.kyoto-u.ac.jp |
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Abstract: | Alzheimer's disease and cerebral amyloid angiopathy are characterized by the deposition of beta-amyloid fibrils consisting of 40- and 42-mer peptides (A beta 40 and A beta 42). Since the aggregation (fibrilization) of these peptides is closely related to the pathogenesis of these diseases, numerous structural analyses of A beta 40 and A beta 42 fibrils have been carried out. A beta 42 plays a more important role in the pathogenesis of these diseases since its aggregative ability and neurotoxicity are considerably greater than those of A beta 40. This review summarizes mainly our own recent findings from the structural analysis of A beta 42 fibrils and discusses its relevance to their neurotoxicity in vitro. |
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