P-77 梯子状ポリエーテル化合物と膜タンパク質の相互作用解析(ポスター発表の部)

概要

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Ladder-shaped polyether (LSP) compounds, such as brevetoxins and ciguatoxins, are thought to interact with a common motif generally occurring in membrane proteins. In this study, to examine the above hypothesis, we assessed the interactions between polycyclic ethers and various proteins using surface plasmon resonance (SPR), SDS-PAGE and NMR experiments. SPR experiments showed that membrane proteins containing transmembrane α-helices had significant affinity for yessotoxin (YTX) and a desulfated derivative (dsYTX) with the dissociation constants of about 10-100μM, whereas water-soluble proteins and a membrane protein forming a β-sheet showed relatively weak affinity for YTX and dsYTX. These results suggest that LSPs recognize membrane proteins, particularly transmembrane α-helix. Then, we examined the influence of molecular length of LSP on the affinity using SPR and SDS-PAGE. In order to specifically observe the effects of molecular length, artificial mono, tetra, hepta and deca cyclic ether (ALPs 1, 4, 7 and 10a) were synthesized and used in the experiments. The results thus obtained revealed that the affinity to transmembrane α-helix increases with increasing molecular length. In addition, decacyclic ALP10b that has four hydroxyl groups on both molecular termini was found to precipitate some membrane proteins, which may be due to specific intermolecular recognitions unique to ALP10b.
天然有機化合物討論会の論文
2007-08-24