Binding Interaction of Dopamine with Bovine Serum Albumin: A Biochemical Study

The binding interaction of bovine serum albumin (BSA) with dopamine was studied by different spectroscopic techniques, and a fluorescence quenching mechanism was associated with this process. Estimated thermodynamic parameters indicated the presence of hydrogen bonding and van der Walls forces between dopamine and BSA. The microenvironment of the protein-binding site was studied by the synchronous fluorescence, FT-TR, and three-way fluorescence techniques in the presence of dopamine, and changes in conformation were indicated within the binding cavity. This study provides useful information on the transportation and distribution of dopamine in proteins.