Tomoko Ueda

Preparation of phospholipid polymers and their properties as polymer hydrogel membranes.

A methacrylate monomer having the phospholipid polar group, 2-methacryloyloxyethyl phosphorylcholine (MPC) was prepared by an improved method with good yield. MPC was copolymerized with n-butyl methacrylate (BMA). The polymer membranes were prepared from the poly(MPC-co-BMA) by a solution casting method. The membrane adsorbed water well and became a hydrogel structure even MPC mole fraction in the copolymer was 0.04. The water content of the hydrogel membrane increased with increase of MPC units and rise of temperature. These properties of the hydrogel membrane were attributed to the highly hydrophilic phospholipid polar group in the copolymer. Water soluble organic compounds and proteins whose molecular weights were below 104 permeated through the hydrogel membrane. However, the protein could not permeate when the molecular weight was higher than 105.

Protein adsorption on biomedical polymers with a phosphorylcholine moiety adsorbed with phospholipid

The effects of phospholipid adsorption onto the polymer surface during adsorption of plasma proteins were investigated. When a polymer with the phosphorylcholine moiety, 2-methacryloyloxyethyl phosphorylcholine (MPC) co-polymer, was treated with dipalmitoylphosphatidylcholine (DPPC) liposome solution, an organized adsorption layer of DPPC was formed on the MPC co-polymer surface, which was confirmed by differential scanning calorimetric analysis and X-ray photoelectron spectroscopy. On the other hand, an organized layer of DPPC on poly(n-butyl methacrylate) and poly(2-hydroxyethyl methacrylate) could not be found. The amount of albumin adsorbed on the polymer surfaces was decreased by pretreatment of the surface with DPPC liposome solution in every polymer case. The smallest amount of adsorbed proteins was found on the MPC co-polymer. Protein adsorption on the surface of MPC co-polymers from the plasma was also small. The difference in protein adsorption on the polymers probably reflects the difference in the orientation of the phospholipid molecules which cover the polymer surface.