Amphotericin B-phospholipid covalent conjugates: dependence of membrane-permeabilizing activity on acyl-chain length.
The interaction between amphotericin B and phospholipid upon forming ion channels across a biomembrane was investigated using their covalent conjugates. The membrane permeabilizing activity was greatly affected by the chain length of the fatty acyl groups, suggesting that their interaction is involved in ion channel assemblages.
Matsuoka
Shigeru
S
Department of Chemistry, Graduate School of Science, Osaka University, Osaka 560-0043, Japan.
Matsumori
Nobuaki
N
Murata
Michio
M
D000666:Amphotericin B / Q000737:chemistry* / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D002625:Chemistry, Organic; D007477:Ions; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D055601:Organic Chemistry Phenomena; D010743:Phospholipids / Q000737:chemistry*; D011188:Potassium / Q000737:chemistry
D000900:Anti-Bacterial Agents; D007477:Ions; D010743:Phospholipids; D000666:Amphotericin B; D011188:Potassium