Synergistic interaction of the streptogramins with the ribosome.
Quantitative binding studies of [G-3H]streptogramin A and [G-3H]streptogramin B with high-salt-washed ribosomes were carried out in the presence of a minimum of 10% (v/v) ethanol because of the antibiotic insolubility in water. It was observed that the presence of streptogramin A increases the affinity of [G-3H]streptogramin B for the ribosome. Thus the dissociation constant for [G-3H]-streptogramin B interaction with the ribosome is Kd=13.3 nM in the presence of streptogramin A and Kd=59 nM in its absence. Furthermore the values for the dissociation constants for [G-3H]-streptogramin B interaction in the presence of 50% (v/v) ethanol, were Kd=0.13 micronM in the presence of streptogramin A and Kd=0.70 micronM in its absence. This increased affinity of [G-3H]streptogramin B in the presence of streptogramin A can explain the synergistic effects of mixtures of streptogramins A and B at the ribosome level.
D000900:Anti-Bacterial Agents / Q000378:metabolism*; D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism*; D000431:Ethanol / Q000494:pharmacology; D007700:Kinetics; D010455:Peptides / Q000378:metabolism; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D010455:Peptides; D000431:Ethanol