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  1. D400 創薬科学研究科
  2. D400a 雑誌掲載論文
  3. 学術雑誌

Principal component analysis of data from NMR titration experiment of uniformly 15N labeled amyloid beta (1–42) peptide with osmolytes and phenolic compounds

http://hdl.handle.net/2237/0002001918
http://hdl.handle.net/2237/0002001918
d367c38f-3f00-44c6-bdba-6a2cd12f3a23
名前 / ファイル ライセンス アクション
ArchBB-Iwaya-accepted-fullversion.pdf ArchBB-Iwaya-accepted-fullversion.pdf (1.2 MB)
Item type itemtype_ver1(1)
公開日 2022-01-13
タイトル
タイトル Principal component analysis of data from NMR titration experiment of uniformly 15N labeled amyloid beta (1–42) peptide with osmolytes and phenolic compounds
言語 en
著者 Iwaya, Naoko

× Iwaya, Naoko

en Iwaya, Naoko

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Goda, Natsuko

× Goda, Natsuko

en Goda, Natsuko

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Matsuzaki, Mizuki

× Matsuzaki, Mizuki

en Matsuzaki, Mizuki

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Narita, Akihiro

× Narita, Akihiro

en Narita, Akihiro

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Shigemitsu, Yoshiki

× Shigemitsu, Yoshiki

en Shigemitsu, Yoshiki

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Tenno, Takeshi

× Tenno, Takeshi

en Tenno, Takeshi

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Abe, Yoshito

× Abe, Yoshito

en Abe, Yoshito

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Hoshi, Minako

× Hoshi, Minako

en Hoshi, Minako

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Hiroaki, Hidekazu

× Hiroaki, Hidekazu

en Hiroaki, Hidekazu

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アクセス権
アクセス権 embargoed access
アクセス権URI http://purl.org/coar/access_right/c_f1cf
権利
言語 en
権利情報 © 2020. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
内容記述
内容記述 A simple NMR method to analyze the data obtained by NMR titration experiment of amyloid formation inhibitors against uniformly 15N-labeled amyloid-β 1–42 peptide (Aβ(1–42)) was described. By using solution nuclear magnetic resonance (NMR) measurement, the simplest method for monitoring the effects of Aβ fibrilization inhibitors is the NMR chemical shift perturbation (CSP) experiment using 15N-labeled Aβ(1–42). However, the flexible and dynamic nature of Aβ(1–42) monomer may hamper the interpretation of CSP data. Here we introduced principal component analysis (PCA) for visualizing and analyzing NMR data of Aβ(1–42) in the presence of amyloid inhibitors including high concentration osmolytes. We measured 1H–15N 2D spectra of Aβ(1–42) at various temperatures as well as of Aβ(1–42) with several inhibitors, and subjected all the data to PCA (PCA-HSQC). The PCA diagram succeeded in differentiating the various amyloid inhibitors, including epigallocatechin gallate (EGCg), rosmarinic acid (RA) and curcumin (CUR) from high concentration osmolytes. We hypothesized that the CSPs reflected the conformational equilibrium of intrinsically disordered Aβ(1–42) induced by weak inhibitor binding rather than the specific molecular interactions.
言語 en
内容記述タイプ Abstract
出版者
言語 en
出版者 Elsevier
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
関連情報
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.1016/j.abb.2020.108446
収録物識別子
収録物識別子タイプ PISSN
収録物識別子 0003-9861
書誌情報 en : Archives of Biochemistry and Biophysics

巻 690, p. 108446, 発行日 2020-09-15
ファイル公開日
日付 2022-01-13
日付タイプ Available
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