2(A-2) アンフォテリシンBと膜脂質の相互作用解明 : 固体NMRによるアプローチ(口頭発表の部)

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Two ^<13>C-labeled amphotericin Bs (AmBs) were prepared by biosynthetic methods. We attained the high level incorporation of [u-^<13>C_6]glucose into AmB resulting uniformly ^<13>C labeled [u-^<13>C]AmB (ca. 50% enriched). The site-selective ^<13>C labeled [tri-^<13>C]AmB was prepared by feeding with sodium [3-^<13>C]propionate feeding (ca. 15% enriched). The ^<13>C-^<13>C correlation spectrum of [u-^<13>C]AmB/dilauroylphosphatidylcholine (DLPC) allowed us to assign all ^<13>C signals on AmB in membrane. The ^<13>C-^<31>P REDOR experiments for dimyristoylphosphatidylcholine (DMPC) membrane using [tri-^<13>C]AmB showed the prominent dephasing effects between the phosphate group in PC and C41 carboxyl carbon in the polar head of AmB. In addition, C39/C40 methyl carbons also gave rise to the significant reduction of their ^<13>C NMR peak, implying that the both terminal parts of AmB reside close to the surface of DMPC membrane. Conversely, the same REDOR experiments with use of distearoylphosphatidylcholine (DSPC) showed no dephasing for the C39/C40 methyl signals while a marked reduction of the C41 carbonyl was again observed. These observations should be most reasonably accounted for by the notion that AmB can span across the DMPC membrane with a single-length interaction but cannot across the DSPC membrane due to its greater thickness. These results may provide the first direct spectroscopic evidence for the formation of a single-length channel across biomembrane, which was previously suggested by channel current recording experiments.
天然有機化合物討論会の論文
2004-10-01

2(A-2) アンフォテリシンBと膜脂質の相互作用解明 : 固体NMRによるアプローチ(口頭発表の部)

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