Comparative studies on the interaction of melizide with bovine serum albumin by fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy

The reactionmechanismofMelizide to bovine serumalbuminwas investigated by both fluorescence quenching and synchronous fluorescence spectroscopy in different temperature (293, 303 and 310 K). The results demonstrated that Melizide caused strong fluorescence quenching of bovine serumalbumin by a dynamic quenchingmechanism, during which the hydrophobic interaction played a dominant role in this system. And the order of magnitudes of binding constant is 104, the number of binding site in the system was closed to 1. It also showed that the primary binding site for CFS was sub-hydrophobic domain IIA. The UV-Vis absorption spectra also showed that the quenching process is dynamic quenching.