ABSTRACT
The potential use of liposomes as a delivery system is still limited by the poor understanding of their interaction mechanisms with biological media. In the present work, interaction between bovine albumin (BA) and liposomes was studied using phase transition and dielectric measurements as well as solubilization process using non-ionic detergent octylglucoside (OG). After liposomes were incubated with diluted and concentrated BA, phase transition, characterizing the liposome membrane exhibited a shift towards higher temperatures, together with initiation of multiple phase transitions. The relaxation time of liposome membrane molecules also increased in a concentration-dependent manner. The solubilization profiles of incubated samples also showed remarkable changes, especially in beginning of solubilization stages. Moreover, amount of detergent needed to completely solubilize membrane was also increased. It was concluded that BA significantly altered the physical state of liposome membrane, which may be attributed to BA interaction with liposomes surface and/or by its incorporation within the bilayer membrane.