Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1376605 | Bioorganic & Medicinal Chemistry Letters | 2008 | 5 Pages |
Abstract
Structural analysis of 42-residue amyloid β (Aβ42) aggregates using rotational resonance in solid-state NMR verified that Cβ and/or Cγ of Met-35 and the carboxyl carbon of Ala-42 are proximal enough to form an intramolecular antiparallel β-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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Authors
Yuichi Masuda, Satoko Uemura, Azusa Nakanishi, Ryutaro Ohashi, K. Takegoshi, Takahiko Shimizu, Takuji Shirasawa, Kazuhiro Irie,