Abstract
High-speed atomic force microscopy (HS-AFM) with high spatiotemporal resolution allows for the video imaging of the conformational changes of individual molecules in an observation area in liquid at nanometer-scale spatial resolution. This method verifies the molecular mechanism and reveals the structural dynamics of relevant biomolecules for various biological phenomena. Here, we describe the methods for HS-AFM observation and the analysis of the structural dynamics of individual amyloidogenic protein assemblies using amyloid β 1–42 as an example.
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References
Ando T (2017) Directly watching biomolecules in action by high-speed atomic force microscopy. Biophys Rev 9:421–429. https://doi.org/10.1007/s12551-017-0281-7
Ando T, Uchihashi T, Scheuring S (2014) Filming biomolecular processes by high-speed atomic force microscopy. Chem Rev 114:3120–3188. https://doi.org/10.1021/cr4003837
Ando T, Uchihashi T, Kodera N (2013) High-speed AFM and applications to biomolecular systems. Annu Rev Biophys 42:393–414. https://doi.org/10.1146/annurev-biophys-083012-130324
Uchihashi T, Kodera N, Ando T (2012) Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy. Nat Protoc 7:1193–1206. https://doi.org/10.1038/nprot.2012.047
Ando T, Uchihashi T, Fukuma T (2008) High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes. Prog Surf Sci 83:337–437. https://doi.org/10.1016/j.progsurf.2008.09.001
Watanabe-Nakayama T, Itami M, Kodera N et al (2016) High-speed atomic force microscopy reveals strongly polarized movement of clostridial collagenase along collagen fibrils. Sci Rep 6:28975. https://doi.org/10.1038/srep28975
Shao Z, Czajkowsky DM (2003) Inhibition of protein adsorption to muscovite mica by monovalent cations. J Microsc 211:1–7. https://doi.org/10.1046/j.1365-2818.2003.01208.x
Yamamoto D, Uchihashi T, Kodera N et al (2010) High-speed atomic force microscopy techniques for observing dynamic biomolecular processes. Methods Enzymol 475:541–564. https://doi.org/10.1016/S0076-6879(10)75020-5
Watanabe-Nakayama T, Ono K, Itami M et al (2016) High-speed atomic force microscopy reveals structural dynamics of amyloid β1-42 aggregates. Proc Natl Acad Sci U S A 113:5835–5840. https://doi.org/10.1073/pnas.1524807113
Kodera N, Yamamoto D, Ishikawa R, Ando T (2010) Video imaging of walking myosin V by high-speed atomic force microscopy. Nature 468:72–76. https://doi.org/10.1038/nature09450
Yamamoto D, Nagura N, Omote S et al (2009) Streptavidin 2D crystal substrates for visualizing biomolecular processes by atomic force microscopy. Biophys J 97:2358–2367. https://doi.org/10.1016/j.bpj.2009.07.046
Yamamoto D, Uchihashi T, Kodera N, Ando T (2008) Anisotropic diffusion of point defects in a two-dimensional crystal of streptavidin observed by high-speed atomic force microscopy. Nanotechnology 19:384009. https://doi.org/10.1088/0957-4484/19/38/384009
Kodera N, Yamashita H, Ando T (2005) Active damping of the scanner for high-speed atomic force microscopy. Rev Sci Instrum 76:53708. https://doi.org/10.1063/1.1903123
Kodera N, Sakashita M, Ando T (2006) Dynamic proportional-integral-differential controller for high-speed atomic force microscopy. Rev Sci Instrum 77:83704. https://doi.org/10.1063/1.2336113
Teplow DB (2006) Preparation of amyloid β-protein for structural and functional studies. Methods Enzymol 413:20–33. https://doi.org/10.1016/S0076-6879(06)13002-5
Acknowledgments
The authors would like to thank Prof. T. Ando, Prof. T. Uchihashi, Dr. N. Kodera, and Dr. H. Konno for the technical advice concerning our HS-AFM observations.
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Watanabe-Nakayama, T., Ono, K. (2018). High-Speed Atomic Force Microscopy of Individual Amyloidogenic Protein Assemblies. In: Lyubchenko, Y. (eds) Nanoscale Imaging. Methods in Molecular Biology, vol 1814. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-8591-3_12
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DOI: https://doi.org/10.1007/978-1-4939-8591-3_12
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