| アイテムタイプ |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2025-03-13 |
| タイトル |
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タイトル |
Protein?Ligand Interaction Analyses with Nuclear Magnetic Resonance Spectroscopy Enhanced by Dissolution Triplet Dynamic Nuclear Polarization |
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言語 |
en |
| 言語 |
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言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| 著者 |
Miyanishi K.
Sugiki T.
Matsui T.
Ozawa R.
Hatanaka Y.
Enozawa H.
Nakamura Y.
Murata T.
Kagawa A.
Morita Y.
Fujiwara T.
Kitagawa M.
Negoro Makoto
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| 抄録 |
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内容記述タイプ |
Abstract |
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内容記述 |
Solution-state nuclear magnetic resonance spectroscopy (NMR) is a powerful method for the analysis of intermolecular interactions within a biomolecular system. However, low sensitivity is one of the major obstacles of NMR. We improved the sensitivity of solution-state 13C NMR for the observation of intermolecular interactions between protein and ligand using hyperpolarized solution samples at room temperature. Eutectic crystals composed of 13C-salicylic acid and benzoic acid doped with pentacene were hyperpolarized by dynamic nuclear polarization using photoexcited triplet electrons, and a 13C nuclear polarization of 0.72 ± 0.07% was achieved after dissolution. The binding of human serum albumin and 13C-salicylate was observed with several hundred times sensitivity enhancement under mild conditions. The established 13C NMR was applied for pharmaceutical NMR experiments by observation of the partial return of the 13C chemical shift of salicylate by competitive binding with other non-isotope-labeled drugs. |
| 書誌情報 |
The Journal of Physical Chemistry Letters
巻 14,
号 27,
p. 6241-6247,
発行日 2023-07
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| 出版者 |
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出版者 |
ACS Publications |
| ISSN |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
1948-7185 |
| PubMed番号 |
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識別子タイプ |
PMID |
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関連識別子 |
37401781 |
| DOI |
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識別子タイプ |
DOI |
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関連識別子 |
10.1021/acs.jpclett.3c01002 |
