摘要：

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 proteinsurfactant 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 correspon...

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