Changes in the physicochemical properties of transferrin upon chemical derivatization with ceramides

The interaction of native and derivatized transferrin with lecithin, cholesterol and their mixtures was studied using monomolecular layers of phospholipids. Moreover, the thermodynamic parameters corresponding to these interactions: the mixing excess free energy, interaction energy, and interaction parameter were also calculated. The ability of these two proteins to insert into monolayers was studied working at constant area. The formation of aggregates or secondary structures in solution was determined by the fluorescence and polarization values of ANS (anilinonaphthalene sulfonate), measured at different protein/ANS relationships.