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.
|Number of pages
|Yuki Gosei Kagaku Kyokaishi/Journal of Synthetic Organic Chemistry
|Published - Dec 2009
All Science Journal Classification (ASJC) codes
- Organic Chemistry