Single-molecule anatomy by atomic force microscopy and recognition imaging

DOI Web Site 被引用文献2件 参考文献84件
  • Takahashi Hirohide
    Laboratory of Plasma Membrane and Nuclear Signaling, Kyoto University Graduate School of Biostudies
  • Hizume Kohji
    Division of Microbial Genetics, National Institute of Genetics, Research Organization of Information and Systems
  • Kumeta Masahiro
    Laboratory of Plasma Membrane and Nuclear Signaling, Kyoto University Graduate School of Biostudies
  • H. Yoshimura Shige
    Laboratory of Plasma Membrane and Nuclear Signaling, Kyoto University Graduate School of Biostudies
  • Takeyasu Kunio
    Laboratory of Plasma Membrane and Nuclear Signaling, Kyoto University Graduate School of Biostudies

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Atomic force microscopy (AFM) has been a useful technique to visualize cellular and molecular structures at single-molecule resolution. The combination of imaging and force modes has also allowed the characterization of physical properties of biological macromolecules in relation to their structures. Furthermore, recognition imaging, which is obtained under the TRECTM (Topography and RECognition) mode of AFM, can map a specific protein of interest within an AFM image. In this study, we first demonstrated structural properties of purified α Actinin-4 by conventional AFM. Since this molecule is an actin binding protein that cross-bridges actin filaments and anchors it to integrin via tailin-vinculin-α actinin adaptor-interaction, we investigated their structural properties using the recognition mode of AFM. For this purpose, we attached an anti-α Actinin-4 monoclonal antibody to the AFM cantilever and performed recognition imaging against α Actinin-4. We finally succeeded in mapping the epitopic region within the α Actinin-4 molecule. Thus, recognition imaging using an antibody coupled AFM cantilever will be useful for single-molecule anatomy of biological macromolecules and structures.

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