Add time:09/26/2019 Source:sciencedirect.com
In this study, the interaction of amphotericin B with human and bovine serum albumins has been investigated by fluorescence spectroscopy. Due to the limitations of several analytical methods by the known aggregation of amphotericin B molecules in aqueous solutions, fluorescence polarization technique was employed to determine complex stabilities. Besides the quantitation of reliable stability constants, this method was found to be able determine the stable aggregated amphotericin B fraction in the presence of serum albumins. Our results demonstrate the formation of highly stable albumin-drug complexes, suggesting the significant role of serum albumins regarding the plasma protein binding of amphotericin B.
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