Study of protein-assemble/disassemble on biological membrane depending on the membrane shape by high-speed AFM
| Project/Area Number |
15H04360
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Kanazawa University |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥16,120,000 (Direct Cost: ¥12,400,000、Indirect Cost: ¥3,720,000)
Fiscal Year 2017: ¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2016: ¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2015: ¥6,500,000 (Direct Cost: ¥5,000,000、Indirect Cost: ¥1,500,000)
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| Keywords | 一分子イメージング / 高速AFM / 生体膜 / 膜タンパク質 / 生体分子 / 生物物理 / 一分子計測（SMD) / 走査プローブ顕微鏡 / タンパク質 |
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| Outline of Final Research Achievements |
Biological membranes have uneven physical shapes. By recognizing on the physical shapes, lipids and proteins specifically assemble and disassemble, and realize their sophisticated functions. In this research project, to realize the real-time observations of these biological processes by high-speed AFM, new AFM substrates with sub-micrometer sized holes have been developed on a glass and PDMS surfaces using Focused Ion Beam (FIB) lithography and nanosphere imprinting. Using the AFM substrates developed here, some phenomena and objects depending on the physical shapes of membrane, diffusion of lipid molecules, assembling of a membrane protein as well as a suspended native membrane, were directly visualized.
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Report
(4 results)
Research Products
(76 results)
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[Journal Article] High-Speed Atomic Force Microscopy Reveals Loss of Nuclear Pore Resilience as a Dying Code in Colorectal Cancer Cells.2017
Author(s)
Mohamed MS, Kobayashi A, Taoka A, Watanabe-Nakayama T, Kikuchi Y, Hazawa M, Minamoto T, Fukumori Y, Kodera N, Uchihashi T, Ando T, Wong RW
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Journal Title
ACS Nano.
Volume: 11(6)
Issue: 6
Pages: 5567-5578
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Mutually exclusive cooperative binding of myosin and cofilin to actin filaments involves cooperative conformational changes of actin.2016
Author(s)
Ngo KX, Umeki N, Kijima ST, Kodera N, Ueno H, Furutani-Umezu N, Nakajima J, Noguchi TQP, Nagasaki A, Tokuraku K, Uyeda TQP
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Journal Title
Scientific Reports
Volume: 6
Issue: 1
Pages: 35449-35449
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Presentation] Physical heterogeneity of bacterial membrane vesicles revealed by high-speed AFM2017
Author(s)
Yousuke Kikuchi, Tatunori Kiyokawa, Kana Morinaga, Yuuma Susa, Yasuda Marina, Hibiki Okuwaki, Ryukou Souma, Nozomu Obana, Masanori Toyohuku, Nobuhiko Nomura, Noriyuki Kodera, Toshio Ando, Yoshihiro Fukumori, Azuma Taoka
Organizer
第55回日本生物物理学会年会
Related Report
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[Presentation] Loss of Nuclear Pore Selective Barrier Revealed by High-Speed Atomic Force Microscopy in Colorectal Cancer Cells2017
Author(s)
Mahmoud Shaaban Mohamed, Akiko Kobayashi, Azuma Taoka, Takahiro Watanabe-Nakayama, Yosuke Kikuchi, Masaharu Hazawa, Toshinari Minamoto, Yoshihiro Fukumori, Noriyuki Kodera, Takayuki Uchihashi, Toshio Ando, Richard Wong
Organizer
第55回日本生物物理学会年会
Related Report
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[Presentation] Structural polymorphism of actin filaments: its implication in regulation of actin binding proteins and cell motility2016
Author(s)
Uyeda, T.Q.P., Ngo, K.X., Noguchi, T.Q.P., Nagasaki, A., Kodera, N., Tokuraku, K.
Organizer
第54回日本生物物理学会年会
Place of Presentation
つくば国際会議場
Year and Date
2016-11-25
Related Report
Invited
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