Dominant formation of a single-length channel by amphotericin B in dimyristoylphosphatidylcholine membrane evidenced by 13C- 31P rotational echo double resonance

Shigeru Matsuoka, Hiroki Ikeuchi, Nobuaki Matsumori, Michio Murata

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13C-Labeled amphotericin B (AmB) was prepared by feeding the producing organism Streptomyces nodosus with [3-13C]propionate. The REDOR experiments for dimyristoylphosphatidylcholine (DMPC) membrane using the 13C-labeled AmB showed the prominent dephasing effects between the phosphate group in PC and C41 carboxyl carbon in the polar head. In addition, C39/C40 methyl carbons also gave rise to the significant reduction of their 13C NMR signals, implying that both terminal parts of AmB reside close to the surface of the 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 signal was again observed. These findings should be most reasonably accounted for by the notion that AmB can span across the DMPC membrane with a single-length interaction but cannot span the DSPC membrane due to its greater thickness. To our knowledge, the results provide the first direct spectroscopic evidence for the formation of a single-length channel across a biomembrane, which was previously suggested by channel current recording experiments.

Original languageEnglish
Pages (from-to)704-710
Number of pages7
Issue number2
Publication statusPublished - Jan 18 2005
Externally publishedYes


All Science Journal Classification (ASJC) codes

  • Biochemistry

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