Aggregation of sodium dodecyl sulfate in micellar solution of (beta)-casein analyzed by 1H NMR self-diffusion, relaxation and Fourier transform IR spectroscopy

Micellization of anionic sodium dodecyl sulfate (SDS) in the presence of -casein (-CN) micelles in aqueous media was studied by 1H NMR and Fourier transform IR spectroscopy. t Alow concentrations SDS molecules incorporate into -CN micelles and modify the protein secondary structure, increasing the portion of helical domains. It was shown that SDS micelles do not appear until binding sites located in the hydrophobic core of -CN micelles are saturated.