Design and Synthesis of Ladder-Shaped Polyethers and Evaluation of the Interaction with Transmembrane Proteins
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- Oishi Tohru
- Graduate School of Science, Osaka University
Bibliographic Information
- Other Title
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- 膜タンパク質との相互作用解明を志向した梯子状ポリエーテルの設計・合成・活性評価
- マク タンパクシツ ト ノ ソウゴ サヨウ カイメイ オ シコウ シタ ハシゴジョウ ポリエーテル ノ セッケイ ゴウセイ カッセイ ヒョウカ
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Abstract
Ladder–shaped polyether (LSP) toxins are thought to bind to transmembrane (TM) proteins. To elucidate the interactions of LSPs with TM proteins, artificial ladder–shaped polyethers (ALPs) possessing simple iterative structure with different number of rings were synthesized based on the convergent method via α–cyano ethers. The interaction of these ALPs with TM proteins was evaluated, and we found that the difference of activities among the ALPs can be accounted for by the concept of “hydrophobic matching” i. e. lengths of the hydrophobic region including the side chains of ALPs are ca. 25 Å, which match the lengths of the hydrophobic region of α–helical TM proteins. The partial structure corresponding to the WXYZA’B’C’ ring system of maitotoxin (MTX) was synthesized based on the convergent method via α–cyano ethers, and we found that hemolysis of human red blood cells induced by MTX was blocked by the fragment. The hydrophobic portion of MTX is expected to be promising molecular probes for identifying the target proteins of MTX.
Journal
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- Journal of Synthetic Organic Chemistry, Japan
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Journal of Synthetic Organic Chemistry, Japan 67 (12), 1250-1260, 2009
The Society of Synthetic Organic Chemistry, Japan
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Keywords
Details 詳細情報について
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- CRID
- 1390001205312516480
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- NII Article ID
- 10026867148
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- NII Book ID
- AN0024521X
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- COI
- 1:CAS:528:DC%2BD1MXhsF2htL7I
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- ISSN
- 18836526
- 00379980
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- NDL BIB ID
- 10520355
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed