Adsorption of glucose oxidase onto plasma-polymerized film characterized by atomic force microscopy, quartz crystal microbalance, and electrochemical measurement.
Adsorption of glucose oxidase (GOD) onto plasma-polymerized thin films (PPF) with nanoscale thickness was characterized by atomic force microscopy (AFM), quartz crystal microbalance (QCM), and electrochemical measurements. The PPF surface is very flat (less than 1-nm roughness), and its properties (charge and wettability) can be easily changed while retaining the backbone structure. We focused on three types of surfaces: (1) the pristine surface of hexamethyldisiloxane (HMDS) PPF (hydrophobic and neutral surface), (2) an HMDS PPF surface with nitrogen-plasma treatment (hydrophilic and positive-charged surface), and (3) an HMDS PPF surface treated with oxygen plasma (hydrophilic and negative-charged surface). The AFM image showed that the GOD molecules were densely adsorbed onto surface 2 and that individual GOD molecules could be observed. The longer axis of GOD ellipsoid molecules were aligned parallel to the surface, called the "lying position", because of electrostatic association. On surface 1, clusters of GOD molecules did not completely cover the original PPF surface (surface coverage was ca. 60%). The 10-nm-size step height between the GOD clusters and the PPF surface suggests that the longer axes of individual GOD molecules were aligned perpendicular to the surface, called the "standing position". On surface 3, only a few of the GOD molecules were adsorbed because of electrostatic repulsion. These results indicate that the plasma polymerization process can facilitate enhancement or reduction of protein adsorption. The AFM images show a corresponding tendency with the QCM profiles. The QCM data indicate that the adsorption behavior obeys the Langmuir isotherm equation. The amperometric biosensor characteristics of the GOD-adsorbed PPF on a platinum electrode showed an increment in the current because of enzymatic reaction with glucose addition, indicating that enzyme activity was mostly retained in spite of irreversible adsorption.
Muguruma
Hitoshi
H
Faculty of Engineering, Shibaura Institute of Technology, 3-7-5 Toyosu, Koto-ku, Tokyo 1358-8548, Japan. muguruma@sic.shibaura-it.ac.jp
Kase
Yoshihiro
Y
Murata
Naoya
N
Matsumura
Kazunari
K
D000327:Adsorption; D005949:Glucose Oxidase / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D011108:Polymers / Q000737:chemistry*; D011791:Quartz / Q000737:chemistry*
D011108:Polymers; D011791:Quartz; D005949:Glucose Oxidase