Adsorption–Desorption of proteins on phospholipid polymer surfaces evaluated by dynamic contact angle measurement

Authors

  • Tomoko Ueda,

    1. Institute for Medical and Dental Engineering, Tokyo Medical and Dental University, 2–3–10, Kanda-Surugadai, Chiyoda-Ku, Tokyo 101, Japan
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  • Kazuhiko Ishihara,

    Corresponding author
    1. Institute for Medical and Dental Engineering, Tokyo Medical and Dental University, 2–3–10, Kanda-Surugadai, Chiyoda-Ku, Tokyo 101, Japan
    • Institute for Medical and Dental Engineering, Tokyo Medical and Dental University, 2–3–10, Kanda-Surugadai, Chiyoda-Ku, Tokyo 101, Japan
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  • Nobuo Nakabayashi

    1. Institute for Medical and Dental Engineering, Tokyo Medical and Dental University, 2–3–10, Kanda-Surugadai, Chiyoda-Ku, Tokyo 101, Japan
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Abstract

Adsorption-desorption of plasma protein on various polymer membranes was evaluated by a dynamic contact angle (DCA) measurement using the Wilhelmy plate method. Poly(ethylene terephthalate) (PET) was used as a substrate membrane; we examined this membrane coated with hydrophilic polymers such as poly[2-methacryloyloxyethyl phosphorylcholine (MPC)-co-n-butyl methacrylate (BMA)] or poly[2-hydroxyethyl methacrylate (HEMA)]. Although the λ-potential of the PET membrane was negative, the coating with poly(MPC-co-BMA) induced increase of value to nearly zero. The DCA loops observed on the polymer membranes after protein adsorption were unity and hysteresis of the loop was reduced. In the cases of protein adsorbed on both the PET and the poly(HEMA) membranes, the shape and hysteresis of the loops were almost same during the rinsing process with a phosphate-buffered solution (PBS). However, the hysteresis of the DCA loops that appeared on the protein-adsorbed poly(MPC-co-BMA) membrane became large during the rinsing process with the PBS, and the shape of the DCA loop returned to its non-protein-adsorbed state. Therefore, proteins adsorbed on poly(MPC-co-BMA) could desorb more readily than those on PET and poly(HEMA) because of the weak interaction between poly(MPC-co-BMA) and the proteins. © 1995 John Wiley & Sons, Inc.

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