Verification of the Intermolecular Parallel .BETA.-Sheet in E22K-A.BETA.42 Aggregates by Solid-State NMR Using Rotational Resonance: Implications for the Supramolecular Arrangement of the Toxic Conformer of A.BETA.42

• MASUDA Yuichi

  Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• NAKANISHI Azusa

  Department of Chemistry, Graduate School of Science, Kyoto University

• OHASHI Ryutaro

  Department of Chemistry, Graduate School of Science, Kyoto University

• TAKEGOSHI Kiyonori

  Department of Chemistry, Graduate School of Science, Kyoto University

• SHIMIZU Takahiko

  Research Team for Molecular Biomarkers, Tokyo Metropolitan Institute of Gerontology Applied Biological Chemistry, United Graduate School of Agricultural Science, Tokyo University of Agriculture and Technology

• SHIRASAWA Takuji

  Research Team for Molecular Biomarkers, Tokyo Metropolitan Institute of Gerontology Department of Ageing Control Medicine, Juntendo University Graduate School of Medicine

• IRIE Kazuhiro

  Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

Bibliographic Information

Other Title

• Verification of the intermolecular parallel β-sheet in E22K-Aβ42 aggregates by solid-state NMR using rotational resonance: implications for the supramolecular arrangement of the toxic conformer of Aβ42
• Verification of the intermolecular parallel v sheet in E22K Av42 aggregates by solid state NMR using rotational resonance implications for the supramolecular arrangement of the toxic conformer of Av42

Abstract

Formation of the intermolecular β-sheet is a key event in the aggregation of 42-residue amyloid-β (Aβ42). We have recently identified a physiological and toxic conformer, the turn positions of which are slightly different from each other, in the aggregates of E22K-Aβ42 (one of the mutants related to cerebral amyloid angiopathy). However, it remains unclear whether the intermolecular β-sheet in the E22K-Aβ42 aggregates is parallel or antiparallel. We prepared an equal mixture of E22K-Aβ42 aggregates labeled at C_α and those labeled at C=O with ¹³C, whose intermolecular ¹³C–¹³C distance was estimated by solid-state NMR using rotational resonance (R2). The intermolecular proximity of β-strands at positions 21 and 30 was less than 6 Å, supporting the existence of the intermolecular parallel β-sheet in the E22K-Aβ42 aggregates as well as in wild-type Aβ42 aggregates. The results also suggest that each conformer would not accumulate alternately, but form a relatively large assembly.

Journal

• Bioscience, Biotechnology, and Biochemistry

  Bioscience, Biotechnology, and Biochemistry 72 (8), 2170-2175, 2008

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• Aβ42
• Alzheimer’s disease
• intermolecular parallel β-sheet
• Italian mutation
• solid-state NMR

Details

• CRID: 1390282681456427264
• NII Article ID: 10027531218
• NII Book ID: AA10824164
• DOI: 10.1271/bbb.80250
• ISSN: 13476947
• ISSN: 09168451
• NDL BIB ID: 9628099
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I9628099
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.80250
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed