albumin - publications
EPR and Circular Dichroism Solution Studies on the Interactions of Bovine Serum Albumin with Ionic Surfactants and β-Cyclodextrin.
J Phys Chem B. 2012 Nov 19;
Authors: Rogozea A, Matei I, Turcu IM, Ionita G, Sahini VE, Salifoglou A
The interactions of bovine serum albumin (BSA) with ionic surfactants (sodium dodecyl sulphate - SDS and cetyltrimethylammonium bromide - CTAB) and β-cyclodextrin (β-CD) have been investigated by electron paramagnetic resonance (EPR) and circular dichroism measurements. The spin probe selected to report on the interaction of albumin with surfactants and/or β-CD was 4-N,N-dimethyl-alkyl-ammonium-2,2,6,6-tetramethyl-piperidine-1-oxyl iodide (CAT16), on account of a) its balance between the electrostatic and hydrophobic character, and b) the ability of BSA to form complexes with various organic molecules. The distribution of the spin probe among different environments in solutions containing only BSA has been confirmed by the existence of two components in the EPR spectra: one revealing a restricted mobility of the spin probe, attributed to the protein-spin probe complex, and another one showing free movement, attributed to the spin probe in solution. The presence of surfactants and/or β-CD alters the distribution of CAT16 between various compartments in each system. Formation of protein aggregates as a result of thermal denaturation was evidenced by the appearance of an immobilized component in the EPR spectrum. This component is not present in the EPR spectra of CAT16 in protein/surfactant or protein/cyclodextrin solutions. Circular Dichroism spectra of BSA provided information about changes in the secondary structure of the protein induced by the presence of surfactants and/or cyclodextrin in solution. The results demonstrate that β-CD hinders the interaction between the employed surfactants and the protein. The cationic surfactant (CTAB) induces changes in protein conformation at a lower concentration compared to the anionic surfactant (SDS).
PMID: 23163315 [PubMed - as supplied by publisher]