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大学・研究所にある論文を検索できる 「Principal component analysis of data from NMR titration experiment of uniformly 15N labeled amyloid beta (1–42) peptide with osmolytes and phenolic compounds」の論文概要。リケラボ論文検索は、全国の大学リポジトリにある学位論文・教授論文を一括検索できる論文検索サービスです。
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Principal component analysis of data from NMR titration experiment of uniformly 15N labeled amyloid beta (1–42) peptide with osmolytes and phenolic compounds

Iwaya, Naoko Goda, Natsuko Matsuzaki, Mizuki Narita, Akihiro Shigemitsu, Yoshiki Tenno, Takeshi Abe, Yoshito Hoshi, Minako Hiroaki, Hidekazu 名古屋大学

2020.09.15

概要

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.

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