抄録
Biointerface for highly sensitive immunoassay was constructed by molecular integration between a phospholipid polymer platform and an antibody as a bioaffinity ligand. The phospholipid polymer platform with nanometer-scaled particle deposition surface was constructed with poly[2-methacryloyloxyethyl phosphorylcholine (MPC)-co-n-butyl methacrylate (BMA)-co-p-nitrophenyloxycarbonyl poly(ethylene glycol) methacrylate (MEONP)] (PMBN) by an electrospray deposition (ESD) method. The PMBN surface, which can conjugate the antibodies, prevented the nonspecific protein adsorption. However, the nanometer-scaled structure of PMBN lost their shape after contact with an aqueous medium. To stabilize the nanometer-scaled structure in an aqueous medium, the PMBN was cross-linked with 1,4-butylenediamine and then heating was applied. Both cross-linking of PMBN and heating were very effective for improving the water stability of the nanometer-scaled structure, that is, remaining high porosity even after immersing in water. The specific signal in the enzyme-linked immunosorbent assay (ELISA) was enhanced after improvement of water stability of the PMBN platform. We concluded that the stabilization of the nanometer-scaled structure of the platform against water was effective to obtain highly sensitive immunoassay.
