Protein adsorption and platelet adhesion on polymer surfaces having phospholipid polar group connected with oxyethylene chain.

We evaluated the blood compatibility of various amphiphilic polymers, that is, n-butyl methacrylate (BMA) copolymers with methacrylates having a phosphorylcholine (PC), hydroxy (OH) or methoxy (MeO) group as an end polar group in the oxyethylene side chain. The amount of proteins adsorbed on the PC-polymer from human plasma was smaller than that on not only the poly(2-hydroxyethyl methacrylate) and poly(methyl methacrylate) but also the OH-polymer and MeO-polymer. The PC group could weaken the interaction between plasma proteins and polymer surfaces. The amount of adsorbed proteins on the PC-polymer decreased with an increase in the mole fraction of the PC units in the polymers. We could observe an effect of the oxyethylene chain length (n is the number of repeating units of oxyethylene) on protein adsorption between n = 2 and n = 3. The platelet adhesion on these polymer surfaces was evaluated using rabbit platelet-rich plasma. On the polymers without the PC group, that is, poly(BMA), OH-polymer, and MeO-polymer, many platelets adhered and a considerable shape change in the adherent platelets occurred. On the other hand, the PC-polymers could effectively suppress platelet adhesion. The platelet adhesion behavior on the polymers was strongly dependent on the adsorbed proteins. Platelet adhesion was completely inhibited on all of the PC-polymers studied having a 0.3 PC unit mole fraction. However, it was observed that the oxyethylene chains on the PC-polymers with a 0.1 PC unit mole fraction affected platelet adhesion.