期刊
NATURE MATERIALS
卷 13, 期 3, 页码 265-271出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NMAT3847
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资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- SENTAN Program of the Japan Science and Technology Agency
- Global COE Program of the Japanese Society for the Promotion of Science
- Japan Society for the Promotion of Science Fellowship
- Grants-in-Aid for Scientific Research [25286057] Funding Source: KAKEN
The conformational flexibility of antibodies in solution directly affects their immune function. Namely, the flexible hinge regions of immunoglobulin G (IgG) antibodies are essential in epitope-specific antigen recognition and biological effector function. The antibody structure, which is strongly related to its functions, has been partially revealed by electron microscopy(1-4) and X-ray crystallography(5,6), but only under non-physiological conditions. Here we observed monoclonal IgG antibodies in aqueous solution by high-resolution frequency modulation atomic force microscopy(7,8) (FM-AFM). We found that monoclonal antibodies self-assemble into hexamers, which form two-dimensional crystals in aqueous solution. Furthermore, by directly observing antibody-antigen interactions using FM-AFM, we revealed that IgG molecules in the crystal retain immunoactivity. As the self-assembled monolayer crystal of antibodies retains immunoactivity at a neutral pH and is functionally stable at a wide range of pH and temperature, the antibody crystal is applicable to new biotechnological platforms for biosensors or bioassays.
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