Competitive Interactions of Ionic Surfactants with Salbutamol and Bovine Serum Albumin: A Molecular Spectroscopy Study with Implications for Salbutamol in Food Analysis

The effect of ionic surfactants, sodium dodecyl sulfate (SDS) and N-cetyl-N,N,N-trimethylammonium bromide (CTAB), on the interaction between beta-agonist salbutamol (SAL) and bovine serum albumin (BSA) was investigated with the use of fluorescence spectroscopy (FLS) and chemometrics methods [multivariate curve resolution-alternating least-squares (MCR-ALS) and parallel factor analysis algorithm (PARAFAC)]. It was found that the binding constant of SAL to BSA in the presence of CTAB was much larger than that without this ligand. The ligand/BSA stoichiometry was 4:1, that is, (CTAB)4 BSA, and was 2:1 with the ligand, that is, (SAL)2 BSA. These results were obtained from the concentration profiles extracted by MCR-ALS for all three reactants. Quantitative information on the complex CTAB BSA SAL species was obtained with the resolution of the excitation emission fluorescence three-way data matrices by PARAFAC. This research has implications for the analysis of SAL in food and might be performed in laboratories associated with organizations such as the U.S. Food and Drug Administration (FDA) and the International Olympic Committee (IOC).