2. Academic Validation
  3. Possible conformation of amphotericin B dimer in membrane-bound assembly as deduced from solid-state NMR

Possible conformation of amphotericin B dimer in membrane-bound assembly as deduced from solid-state NMR

  • Bioorg Med Chem. 2012 Oct 1;20(19):5699-704. doi: 10.1016/j.bmc.2012.08.016.
Yuichi Umegawa 1,  Takeshi Adachi,  Nobuaki Matsumori,  Michio Murata
Affiliations

Affiliation

  • 1 Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
PMID: 22959766 DOI: 10.1016/j.bmc.2012.08.016
Abstract

Aiming for structural analysis of amphotericin B (AmB) ion-channel assemblies in membrane, a covalent dimer was synthesized between (13)C-labled AmB methyl ester and (19)F-labled AmB. The dimer showed slightly weaker but significant biological activities against fungi and red blood cells compared with those of monomeric AmB. Then the dimer was subjected to (13)C{(19)F}REDOR (Rotational-Echo Double Resonance) experiments in hydrated lipid bilayers. The obtained REDOR dephasing effects were explained by two components; a short (13)C/(19)F distance (6.9Å) accounting for 23% of the REDOR dephasing, and a longer one (14Å) comprising the rest of the dephasing. The shorter distance is likely to reflect the formation of barrel-stave ion channel.

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