The effect of albumin on incorporation of merocyanine 540 into phospholipid liposomes.

Absorption and fluorescence emission spectroscopy was applied to study the changes in albumin modified incorporation of merocyanine 540 into liposomes composed of different lecithins (DMPC, DPPC, POPC, and egg PC). Our results confirmed high affinity of merocyanine molecules toward albumin and revealed that albumin competed with all phospholipids used for binding merocyanine 540 molecules. However, the extent of this competition was determined by the kind of phospholipid. Albumin competed very successfully with lecithins containing saturated fatty acid chains (DPPC, DMPC) and weakly with unsaturated lecithins (POPC, egg PC) for binding merocyanine 540 molecules.