Abstract
Aiming for structural analysis of amphotericin B (AmB) ion-channel assemblies in membrane, a covalent dimer was synthesized between 13C-labled AmB methyl ester and 19F-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 13C{19F}REDOR (Rotational-Echo Double Resonance) experiments in hydrated lipid bilayers. The obtained REDOR dephasing effects were explained by two components; a short 13C/19F 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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