Conformational analysis of a cyclic molecule of channel-forming antibi
otic Amphotericin B (AMP) was conducted by the methods of molecular me
chanics. A number of conformers differing in both hydroxyl group orien
tation and lacton ring conformation were obtained. The stable states o
f the conformers have close values of intrinsic energy. The conformati
onal analysis supports the conclusion of Mazerski J. and Borowski E. (
Biophys. Chem. 1995. V. 54. P. 49) on the flexibility of the AMP lacto
n ring, based on molecular dynamics study.