Abstract
AbstractFluorescence spectra and UV‐Vis absorption spectra have been used to study the binding of bacteriophage mequindox (MEQ) with bovine serum albumin (BSA), which performed a dynamic quenching process. The quenching constants and thermodynamic parameters at different temperatures were calculated. The binding was primarily driven by entropy, and hydrophobic forces also played a significant role. The distance between BSA and MEQ was estimated to be 4.5 nm based on the theory of F?rster's non‐radioactive energy transfer. Furthermore, synchronous fluorescence spectra and 3‐dimensional fluorescence spectra were used to figure out the configuration of BSA in the presence or absence of MEQ, which indicated that it was basically the same.
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