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


J Agric Food Chem. 2013 Jul 22;


Authors: Zhang Q, Ni Y, Kokot S


Abstract

The effect of ionic surfactants, sodium dodecyl sulfate (SDS) and N-cetyl-N,N,N-trimethyl ammonium bromide (CTAB), on the interaction between b-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, i.e. (CTAB)4-BSA and 2:1 with the ligand, i.e. (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 that might be performed by laboratories associated with organizations such as the U.S. Food and Drug Administration (FDA) and the International Olympic Committee (IOC).

PMID: 23875531 [PubMed - as supplied by publisher]