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    Adsorption of Proteins Derived from Fetal Bovine Serum onto Hydroxyapatite Nanocrystals with Quartz Crystal Microbalance Technique

    Year: 2009

    Journal: Key Engineering Materials Vols. 396-398 (2009) pp 47-50, 20110210

    Authors: Tagaya M. 1 2, Ikoma T. 1, Takemura T. 1, Okuda M. 1, Hanagata N. 1, Yoshioka T. 2, Chakarov D. 3, Kasemo B. 3, Tanaka J. 2.

    Last authors: J. Tanaka

    Organizations: 1 Biomaterials Center, National Institute for Materials Science, Sengen 1-2-1,Tsukuba, Ibaraki 305-0047, Japan 2 Graduate School of Science & Engineering, Tokyo Institute of Technology, O-okayama 2-12-1,Meguro-ku, Tokyo 152-8550, Japan 3 Department of Applied Physics, Chalmers University of Technology and Göteberg University,Göteberg, S-412 96, Sweden

    Country: Japan

    The adsorption of multiple proteins derived from fetal bovine serum (FBS) in phosphate buffer saline (PBS) and alpha minimum essential (aMEM) was in situ analyzed with a quartz crystal microbalance with dissipation technique on gold, titanium and HAp sensors. The adsorption behaviors of FBS proteins were varied depending on the sensors. The DD/Df value of the HAp sensor were clearly different in PBS and aMEM, and others were not changed. The viscoelastic properties of the protein films adsorbed on the HAp sensor in PBS were flexible in comparison with those on the gold and titanium sensors. The D-f plots incidated that the proteins adsorbed on HAp in PBS would lead to competitive adsorption and conformational change and those in aMEM could form a monolayer. The adsorption behavior on the HAp in carbonate buffer saline was found to be similar to that in aMEM. These differential adsorption behaviors on the HAp surface were attributed to the pre-adsorptive ion, such PO43- or CO32- in the solvent.

    Keywords: hydroxyapatite (HAp), protein adsorption, QCM-D, biosensor, fetal bovine serum (FBS)