Steady-state and dynamic fluorescence measurements were used to investigate the interactions and
structures of complexes formed between bovine serum albumin (BSA) and anionic, cationic, and nonionic
surfactants: sodium dodecyl sulfate (SDS), N-cetyl-N,N,N-trimethylammonium bromide (CTAB), and
octaoxyethylene glycol n-dodecyl ether (C12E8), respectively. The lysozyme (Lys)−SDS complex was also
studied. The measurements were carried out at different pH's and ionic strengths. In all systems, micelle-like clusters adsorbed on protein were evidenced. The average aggregate numbers are smaller than those
of free micelles and are not strongly influenced by pH and ionic strength. The fluorescence lifetime of
pyrene in BSA/surfactant complexes was constant at low surfactant concentrations, started to decrease
at approximately the same protein−surfactant ratio (0.15 mM BSA/1 mM surfactant) regardless of the
surfactant type or pH buffer, and, at high surfactant concentrations, merged to the lifetime values
corresponding to free micelles. The results of the fluorescence techniques support a “necklace and bead”
model of the complex for BSA/surfactant systems, with protein wrapped around the micelles. For the
Lys/SDS complex, the model essentially is the same; however, some differences, due to their different sizes,
appear. Lysozyme is smaller and more rigid and does not wrap up well around the micelle.