Abstract
Polyene antibiotics can be classified into two major groups based on the size of their macrolide rings [1, 2]. The large polyenes, of which amphotericin B is an example, have seven conjugated double bonds (heptaene), whereas the small polyenes contain fewer than seven double bonds. Nystatin is structurally similar to amphotericin B except that it has four conjugated double bonds and two conjugated bonds separated from the four by a methylene bridge. It has been classified as a large polyene along with amphotericin B [1, 2]. A number of biologic properties distinguish the large polyenes from the small, including the relation between their permeabilizing and lytic actions on cells [1-3]. Here we extend our study of the interactions of lipoproteins with amphotericin B [4] to other polyenes.
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