Efficient Target Protein Labeling by Natural Product-based Molecular Probes : Some Rules for Linker Designing
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- Ebine Makoto
- Graduate School of Science, Tohoku University
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- Inomata Sho
- Graduate School of Science, Tohoku University
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- Nakamura Yoko
- Graduate School of Science, Tohoku University
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- Mukai Makoto
- Graduate School of Science, Tohoku University
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- Ueda Minoru
- Graduate School of Science, Tohoku University
Bibliographic Information
- Other Title
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- P-45 分子プローブによるLCF標的タンパク質の効率的標識化 : リンカー構造の重要性(ポスター発表の部)
Abstract
Nowadays, there are various approaches to study the mechanism of action of a bioactive natural product, and one powerful way is "Activity-based protein profiling (ABPP)". In ABPP, naturally occuring bioactive substances-based molecular probes are employed to elucidate the interecting proteins. For the success in ABPP approach, it is essential to use proper chemical probes with following properties; a) strongly interact with original target protein, b) easily soluble in aqueous medium, c) having low non-specific binding, and so on. It is said, however, that there are no universal guidelines for the design of promising chemical probes and that is an important impediment for ABPP strategy. In the course of our chemical biology studies on jasmonate glycoside, a leaf-closing factor of Samanea saman, we encoutered with an interesting issue that CuAAC-mediated biaryl-linked molecular probe (BArL probe) gives us not only a synthetic convenience but also a higher labeling efficiency. From DFT calculation and NMR analysis, we reasoned its efficiency enlargement that rigid biaryl structure makes the probe conformation rather open form than those without biaryl linkage. Details will be discussed on the poster presentation.
Journal
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- Symposium on the Chemistry of Natural Products, symposium papers
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Symposium on the Chemistry of Natural Products, symposium papers 52 (0), 373-377, 2010
Symposium on the Chemistry of Natural Products Steering Committee
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Details 詳細情報について
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- CRID
- 1390001206077444736
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- NII Article ID
- 110009757787
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- ISSN
- 24331856
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- Text Lang
- ja
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- Data Source
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- JaLC
- CiNii Articles
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- Abstract License Flag
- Disallowed