Multinuclear Dynamic NMR of Diffusion and Transport of Popypeptides by Membrane Thermal Fluctuation
Project/Area Number |
24550035
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Physical chemistry
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Research Institution | Himeji Dokkyo University |
Principal Investigator |
Okamura Emiko 姫路獨協大学, 薬学部, 教授 (00160705)
|
Co-Investigator(Kenkyū-buntansha) |
AKI KENZO 姫路獨協大学, 薬学部, 助手 (50714945)
TAKECHI YUKI (HARAYA YUKI) 姫路獨協大学, 薬学部, 助教 (30634604)
|
Project Period (FY) |
2012-04-01 – 2016-03-31
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Project Status |
Completed (Fiscal Year 2015)
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Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
|
Keywords | 生物物理 / 界面・表面物性 / 超精密解析 / NMR / 膜輸送 / 膜透過 |
Outline of Final Research Achievements |
Molecular dynamics in membrane inside and outside was quantified by multinuclear, dynamic NMR in situ, in relation to the thermal fluctuation of membranes. First, the lipid membrane dynamics was successfully characterized in cell sized vesicles (CSVs) of 10-20 μm-diameters by using solution-state NMR. The dynamic structure of CSVs was found to be different from nano-sized vesicles of ~100 nm-diameters frequently used. The contribution of membrane fluctuation to molecular transport was also quantified in the presence of various amounts of cholesterol in the membrane. The peptide permeation to living cell inside was also observed by real-time in-cell NMR in situ and analyzed by first-order kinetics. Such kinetic approach was also applicable to time-resolved studies of biochemical reactions in peptides such as peptide bond cleavage in human-lens crystallin fragment in situ.
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Report
(5 results)
Research Products
(47 results)
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[Journal Article] Physicochemical Mechanism for the Lipid Membrane Binding of Polyarginine: the Favorable Enthalpy Change with Structural Transition from Random Coil to α-Helix2012
Author(s)
Takechi, Y., Mizuguchi, C., Tanaka, M., Kawakami, T., Aimoto, S., Okamura, E., and Saito, H
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Journal Title
Chem. Lett
Volume: 41(10)
Issue: 10
Pages: 1374-1376
DOI
NAID
Related Report
Peer Reviewed
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