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Title: New diagnostic method for Alzheimer’s disease based on the toxic conformation theory of amyloid β
Authors: Irie, Kazuhiro  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0001-7109-8568 (unconfirmed)
Author's alias: 入江, 一浩
Keywords: Alzheimer’s disease
amyloid β
antibody
protein kinase C
solid-phase peptide synthesis
Issue Date: 2020
Publisher: Japan Society for Bioscience Biotechnology and Agrochemistry
Journal title: Bioscience, Biotechnology and Biochemistry
Volume: 84
Issue: 1
Start page: 1
End page: 16
Abstract: Recent investigations suggest that soluble oligomeric amyloid β (Aβ) species may be involved in early onset of Alzheimer’s disease (AD). Using systematic proline replacement, solid-state NMR, and ESR, we identified a toxic turn at position 22 and 23 of Aβ42, the most potent neurotoxic Aβ species. Through radicalization, the toxic turn can induce formation of the C-terminal hydrophobic core to obtain putative Aβ42 dimers and trimers. Synthesized dimer and trimer models showed that the C-terminal hydrophobic core plays a critical role in the formation of high molecular weight oligomers with neurotoxicity. Accordingly, an anti-toxic turn antibody (24B3) that selectively recognizes a toxic dimer model of E22P-Aβ42 was developed. Sandwich enzyme-linked immunosorbent assay with 24B3 and 82E1 detected a significantly higher ratio of Aβ42 with a toxic turn to total Aβ42 in cerebrospinal fluid of AD patients compared with controls, suggesting that 24B3 could be useful for early onset of AD diagnosis.
Rights: This is an Accepted Manuscript of an article published by Taylor & Francis in Bioscience, Biotechnology and Biochemistry on 20 September 2019, available online: http://www.tandfonline.com/10.1080/09168451.2019.1667222.
The full-text file will be made open to the public on 20 September 2020 in accordance with publisher's 'Terms and Conditions for Self-Archiving'.
この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
This is not the published version. Please cite only the published version.
URI: http://hdl.handle.net/2433/245866
DOI(Published Version): 10.1080/09168451.2019.1667222
PubMed ID: 31538538
Appears in Collections:Journal Articles

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