Study on elementary processes of biomolecule recognition based on control of solid surfaces
| Project/Area Number |
24360013
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Thin film/Surface and interfacial physical properties
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| Research Institution | Yokohama National University |
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Principal Investigator |
OGINO Toshio 横浜国立大学, 工学(系)研究科(研究院), 教授 (70361871)
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| Co-Investigator(Renkei-kenkyūsha) |
URISU Tsuneo 名古屋大学, 工学系研究科, 教授 (50249950)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥19,240,000 (Direct Cost: ¥14,800,000、Indirect Cost: ¥4,440,000)
Fiscal Year 2014: ¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2013: ¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2012: ¥9,620,000 (Direct Cost: ¥7,400,000、Indirect Cost: ¥2,220,000)
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| Keywords | 表面・界面物性 / 吸着 / 生体分子 / グラフェン / エクソソーム / タンパク質 / 固体表面 / バイオセンサ / 表面界面 / バイオテクノロジー / ナノカーボン / 酸化物単結晶 / ナノポアデバイス / 表面化学 |
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| Outline of Final Research Achievements |
Elementary processes of biomolecule and biomaterial recognition on solid surfaces were studied based on structural and chemical control of the substrate surfaces. Ferroelectric materials have been introduced as a new substrate for selective adsorption of protein molecules and found to be promising for new biosensor platforms. We have also found that chemical properties of graphene films can be modulated by modification of the substrate surfaces that immobilize the graphene films. Adsorption properties of exosomes to solid surfaces have been studied by atomic force microscopy, and it has been demonstrated that adsorption types are classified into four modes according to the shapes of the adsorbed exosomes. Ion current drops in the nanopore devises have been successfully observed using polymer beads.
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Report
(4 results)
Research Products
(107 results)
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[Journal Article] Amino and carboxyl terminal domains of Filamin-A interact with CRMP1 to mediate Sema3A-signaling2014
Author(s)
Fumio Nakamura, Kosuke Kumeta, Tomonobu Hida, Toshinari Isono, Yuichi Nakayama, Emiko Kuramata-Matsuoka, Naoya Yamashita, Yutaka Uchida, Ken-ichi Ogura, Keiko Gengyo-Ando, Shohei Mitani, Toshio Ogino, and Yoshio Goshima
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Journal Title
Nat. Commun.
Volume: 5 5325
Issue: 1
Pages: 1-14
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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