Study on the binding of trichloromonofluoromethane by bovine serum albumin using a fluorescent probe technique

Protein binding of the aerosol propellant, trichloromonofluoromethane, was studied in bovine serum albumin (BSA) solutions using the fluorescent probe technique. The propellant displaced the probe, 8-anilino-1-naphthalenesulfonate, from its binding sites and reduced the fluorescence intensity. The binding association constants, the number of binding sites, and the competitive nature of the binding interaction were investigated. The hydrophobic nature of the binding and the implication of binding displacement interactions between the fluorocarbon and plasma-protein-bound drugs were also discussed. The fatty acid impurities present in the commercial BSA were found to have no effect on the protein binding of the propellant.