methylamphotericin-b and Hemolysis

methylamphotericin-b has been researched along with Hemolysis* in 1 studies

Other Studies

1 other study(ies) available for methylamphotericin-b and Hemolysis

Article	Year
Possible conformation of amphotericin B dimer in membrane-bound assembly as deduced from solid-state NMR. Bioorganic & medicinal chemistry, 2012, Oct-01, Volume: 20, Issue:19 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. Topics: Amphotericin B; Antifungal Agents; Aspergillosis; Aspergillus niger; Dimerization; Erythrocytes; Hemolysis; Humans; Lipid Bilayers; Magnetic Resonance Spectroscopy; Molecular Conformation	2012

Article

Year

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

Bioorganic & medicinal chemistry, 2012, Oct-01, Volume: 20, Issue:19

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.

Topics: Amphotericin B; Antifungal Agents; Aspergillosis; Aspergillus niger; Dimerization; Erythrocytes; Hemolysis; Humans; Lipid Bilayers; Magnetic Resonance Spectroscopy; Molecular Conformation

2012