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    Immobilization of carbohydrate clusters on a quartz crystal microbalance sensor surface

    Year: 2013

    Journal: Journal of Colloid and Interface Science Volume 393, 1 March 2013, Pages 257–263, 20130402

    Authors: Masayo Ogiso 1, Koji Matsuoka 2, Tomoko Okada 3, Tomoko Imai 4, Miki Itoh 4, Takeshi Imamura 4, Yoshimi Haga 5, Kenichi Hatanaka 5, Norihiko Minoura 3

    Last authors: Norihiko Minoura

    Organizations: 1 Japan Chemical Innovation Institute, 1-3-5 Jimbocho, Chiyoda-ku, Tokyo 101-0051, Japan 2 Area for Molecular Function, Division of Material Science, Graduate School of Science and Engineering Saitama University, Sakura, Saitama 338-8570, Japan 3 Tokyo University of Technology, School of Bioscience & Biotechnology, 1404-1 Katakura, Hachioji, Tokyo 192-0982, Japan 4 Canon Inc., 30-2, Shimomaruko 3-chome, Ohta-ku, Tokyo 146-8501, Japan 5 Institute of Industrial Science, The University of Tokyo, 4-6-1 Komaba, Meguro-ku, Tokyo 153-8505, Japan

    Country: Japan

    The immobilization of carbohydrates on gold surfaces is a prerequisite technology for carbohydrate-related studies, including those of carbohydrate–biomolecule interactions. Glycolipid domains in cell membranes, such as lipid rafts, are thought to play an important role in cell biology through their carbohydrate portions. To understand the recognition of glycolipid domains such as receptors for bacterial toxins and viruses, we immobilized clusters of carbohydrates on a gold surface by using polyamidoamine (PAMAM) dendrimers as a scaffold. The PAMAM dendrimers were adsorbed on the gold-coated surface of a quartz crystal microbalance (QCM) sensor and were observed by means of QCM with dissipation (QCM-D). After adsorption of the PAMAM dendrimers, lysoganglioside-GM1 and 12-aminododecyl-N-acetylglucosaminide (GlcNAc–C12–NH2) were immobilized on the amino groups of PAMAM dendrimers by means of an NH2 cross-linker. Immobilization of the carbohydrates was confirmed by observation of their specific interaction with anti-ganglioside GM1 antibody or wheat germ agglutinin (WGA). Surfaces with different GlcNAc–C12–NH2 cluster sizes and densities were prepared by varying the size of the PAMAM dendrimers or the concentration of GlcNAc–C12–NH2 immobilized on the dendrimers, respectively. Analysis of the binding between the GlcNAc–C12–NH2-immobilized surface and WGA revealed that the size of the PAMAM dendrimers influenced the GlcNAc–C12–NH2–WGA interaction, with larger dendrimers resulting in higher WGA binding constants.