Detection and control of molecular orientation and reactivity of biomembrane model reaction field including proteins

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I constructed a new biomembranes model system for the investigation of the active structures of lipid molecules which act as reactive factors of membrane proteins at cell membrane reactions. I fabricated a supported lipid bilayer (SLB) including phosphatidylinositol on mica substrate, and found that depression domains with 20 - 300 nm in lateral size and ~0.9 nm in depth in the PI-SLB. In-situ atomic force microscope (AFM) observation revealed that these submicron depression domains acted as the nucleation site of the self-assembly of F-BAR on the PI-SLB, a membrane deformation protein, and the surrounding region of the depression domains provided the F-BAR to the nucleation site. It is a novel result clearly showing the roles of submicron lipid domains during a protein reaction. I also established the fabrication methods of SLBs on graphene oxide and poly vinyl chloride membrane for the development of the methods to evaluate the molecular state and membrane properties in the SLBs.