Verification of the C-terminal intramolecular beta-sheet in Abeta42 aggregates using solid-state NMR: implications for potent neurotoxicity through the formation of radicals |
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Authors: | Masuda Yuichi Uemura Satoko Nakanishi Azusa Ohashi Ryutaro Takegoshi K Shimizu Takahiko Shirasawa Takuji Irie Kazuhiro |
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Institution: | Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan. |
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Abstract: | Structural analysis of 42-residue amyloid beta (Abeta42) aggregates using rotational resonance in solid-state NMR verified that C(beta) and/or C(gamma) of Met-35 and the carboxyl carbon of Ala-42 are proximal enough to form an intramolecular antiparallel beta-sheet in the C-terminus. The S-oxidized radical cation at Met-35, an ultimate radical species responsible for neurotoxicity, could be stabilized by the carboxylate anion at the C-terminus, resulting in aggregation to cause long-term oxidative stress. |
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