Solvation dynamics of LDS 750 in micelles, reverse micelles and proteins

In the present study, steady state, picosecond resolved fluorescence and polarization-gated anisotropy have been used to characterize the binding of LDS 750 (LDS) in biomimetics and in the transporter protein bovine serum albumin (BSA). Competitive binding studies with well-known BSA binding drugs warfarin and diflunisal show that LDS binds in domain III of the protein. Time resolved emission spectra (TRES) have been used to determine the dynamics of environmental relaxation in restricted media. Our studies open the possibility of using the dye as a potential fluorescence and solvation reporter in other proteins and biomimetics of interest.