The Study Of Interaction Between Bovine Serum Albumin And Small Organic Fluorophore

Understanding the strategies for labeling proteins with fluorophores are important in biological studies. Here we take a model protein (bovine serum albumin) and a typical fluorophore (Rhodamine B and Eosin B) to demonstrate a direct labeling just by physical adsorption in macro and micro. In combination with size exclusion chromatography, centrifugal sedimentation and the Scartchard equation, we have developed a facile analysis method of successfully calculating the affinity constant and binding sites. In addition, the molecular docking method was also employed to further studying the binding site on an amino acid level under simulative physiological conditions. In the mean time, we use 3-D fluorescence spectra confirmed the micro-environmental and conformational changes of BSA molecules because of the interaction with the two different fluorophore, and because of the binding site of BSA for Erosin B much more than for Rhodamine B, so the change of conformation of BSA interact with Eosin B is bigger than the interaction changes for Rhodamine B.