Study of the interactions between lysozyme and a fully-fluorinated surfactant in aqueous solution at different surfactant-protein ratios.
The interactions of a fluorinated surfactant, sodium perfluorooctanoate, with lysozyme, have been investigated by a combination of UV absorbance, electrical conductivity and dynamic light scattering to detect and to characterize the conformational transitions of lysozyme. By using difference spectroscopy, the transition was followed as a function of surfactant concentration, and the data were analyzed to obtain the Gibbs energy of the transition in water (DeltaGw(o)) and in a hydrophobic environment (DeltaGh(o)) for saturated protein-surfactant complexes. Electrical conductivity was used to determine the critical micelle concentration of the surfactant in the presence of different lysozyme concentration. From these results, the average number of surfactant monomer per protein molecule was calculated. Finally, dynamic light scattering show that only changes in the secondary structure of the protein can be observed.
Department of Applied Physics, Group of Biophysics and Interfaces, Faculty of Physics, University of Santiago de Compostela, E-15782 Santiago de Compostela, Spain. faruso@usc.es
Juan M
JM
Ruso
Alfredo
A
González-Pérez
Gerardo
G
Prieto
Félix
F
Sarmiento
D002210:Caprylates / Q000737:chemistry*; D002627:Chemistry, Physical / Q000379:methods; D003217:Conductometry / Q000379:methods; D005466:Fluorocarbons / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D012996:Solutions; D014867:Water
D002210:Caprylates; D005466:Fluorocarbons; D012996:Solutions; D014867:Water; C023036:perfluorooctanoic acid; D009113:Muramidase