Smirnov S L
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region.
Membr Cell Biol. 1997;10(5):553-63.
Conformational analysis of a cyclic molecule of a channel-forming antibiotic amphotericin B was conducted by the methods of molecular mechanics. A number of conformers differing in both hydroxyl group orientation and lactone ring conformation were obtained. The stable states of the conformers have close intrinsic energies. The conformational analysis supports the conclusion by Mazerski and Borowski (Biophys. Chem. 54:49-60 (1995)) on the flexibility of the amphotericin B lactone ring.
采用分子力学方法对形成通道的抗生素两性霉素B的环状分子进行了构象分析。获得了许多在羟基取向和内酯环构象上都不同的构象异构体。这些构象异构体的稳定状态具有相近的内在能量。该构象分析支持了Mazerski和Borowski（《生物物理化学》54:49 - 60 (1995)）关于两性霉素B内酯环灵活性的结论。
