Competitive adsorption between phospholipid and plasma protein on a phospholipid polymer surface

The competitive adsorption of proteins and phospholipids on omega-methacryloyloxyalkyl phosphorylcholine (MAPC) polymer was evaluated in this study. Albumin, fibrinogen, and dimyrstoyl phosphatidylcholine (DMPC) were used as model components. The amount of DMPC adsorbed on the MAPC polymers increased with an increase in the MAPC unit composition of the polymer. The methylene chain length of the MAPC unit was another factor influencing the DMPC adsorption when the MAPC unit composition of the MAPC polymer was low. The state of albumin and DMPC liposome adsorbed on the 2-methacryloyloxyethyl phosphorylcholine (MPC) polymer was determined by dynamic contact angle (DCA) measurement. The adsorption strength of albumin on the MPC polymer was weaker than that on the poly[n-butyl methacrylate (BMA)], that is: the albumin was detached from the MPC polymer during the rinsing process. On the poly(BMA) surface, no difference in the shape of the DCA loops before and after contact with the DMPC liposomal suspension was observed. Fibrinogen adsorption on the MAPC polymer was detected by gold-colloid labeled immunoassay. The amount of fibrinogen adsorbed on every MAPC polymer surface was reduced by addition of the DMPC liposome in the fibrinogen solution. The number of platelets adhered on the MAPC polymer was also decreased when the DMPC liposome was present in the fibrinogen solution during pretreatment. We concluded that phospholipids were preferentially adsorbed on the MAPC polymer surface compared with plasma protein and that the adsorbed phospholipids played an important role in showing an excellent blood compatibility on the MAPC polymer.