Studies of binding C3-substitute rifamycins to human and bovine serum albumin.
The interactions of a series of C3-substituted rifamycins with human and bovine serum albumins were studied in order to find possible correlations between the degree of binding and the structural features of the various molecules. The results obtained indicate some of the physicochemical properties and, therefore, of the structural requirements which appear to determine or influence the bonding mechanisms of this series of rifamycins. Two types of interaction were found to exist, ionic and hydrophobic types. The findings suggest that the inhibition by protein of the antibacterial activities of these antibiotics depends on the type of bonding mechanism rather than the degree of binding.
Studies of binding C3-substitute rifamycins to human and bovine serum albumin. The interactions of a series of C3-substituted rifamycins with human and bovine serum albumins were studied in order to find possible correlations between the degree of binding and the structural features of the various molecules. The results obtained indicate some of the physicochemical properties and, therefore, of the structural requirements which appear to determine or influence the bonding mechanisms of this series of rifamycins. Two types of interaction were found to exist, ionic and hydrophobic types. The findings suggest that the inhibition by protein of the antibacterial activities of these antibiotics depends on the type of bonding mechanism rather than the degree of binding.