Surface characterization of Immunoglobulin G and Sodium Perfluorooctanoate mixed solutions by pendant drop tensiometry

GERARDO PRIETO ; PAULA V. MESSINA; ELENA BLANCO; JUAN SABIN; JUAN M RUSO; FÉLIX SARMIENTO

Granada, España

Workshop; International Workshop on Bubble and Drop Interfaces; 2007

Universidad de Granada

Fluorinated amphiphiles consititutes novel and versatile components useful for preparing films and membranes, elaborating and stabilized coloidals systems, coating and dispersing micro and nanoparticles, protecting large bioengineered molecules, modulating the response of temperature and pH-sensitive materials. The fact that stable organization of fluorinated amphiphiles, especially at interfaces, can be achieved for aignificantly shorter chain lenght than for hydrocarbon analogs, permits the access of fluorinated amphiphiles to thinner, yet stable Langmuir-Blodgett monolayers and membranes. In previous works we have studied the interaction of the fluoroamphiphile sodium perfluorooctanoate (SPFO) and the protein human serum albumin (HSA) The interfacial behaviour of mixed immunoglobulin (IgG) and sodium perfluorooctanoate (SPFO) solutions is examined by using pendant drop tensiometry. On consequence of these interactions, the protein structure was affected and also its adsorption at the air-aqueous interface. Experiments over adsorbed and spreading IgG monolayers were been doing. The analysis of adsorbed and spreading SPFO-IgG monolayers, shows that surfactant molecules preferred the bind on IgG structure than the migration to air-aqueous interface. The presence of surfactant molecules affects the adsorption regimes, characteristic of a protein adsorption.