Monomer-collagen interactions studied by saturation transfer difference NMR.
Project/Area Number |
25462951
|
Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Conservative dentistry
|
Research Institution | Tokyo Medical and Dental University |
Principal Investigator |
Hiraishi Noriko 東京医科歯科大学, 大学院医歯学総合研究科, 日本学術振興会特別研究員 (20567747)
|
Project Period (FY) |
2013-04-01 – 2017-03-31
|
Project Status |
Completed (Fiscal Year 2016)
|
Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
|
Keywords | NMR / コラーゲン / 象牙質 / 接着性モノマー / 疎水性結合 / MDP / 31P 固体NMR / 歯科接着性モノマー / HEMA / 核磁気共鳴装置 / レジン |
Outline of Final Research Achievements |
The nteraction of functional adhesive monomers with collagen is not understood at a molecular/atomic level. We performed saturation transfer difference (STD) NMR spectroscopy to investigate the binding interaction of 10-methacryloyloxydecyl dihydrogenphosphate (MDP), with atelocollagen as a triple-helical peptide model. High STD intensities were detected on the protons in the aliphatic region in MDP. The STD results imply that MDP has a relatively stable interaction with the collagen, because of the hydrophobic interactions between the hydrophobic MDP moieties and the hydrophobic collagen surface. This finding indicates that MDP-collagen complexation accounts for stable dentin bonding. Furthermore, we examined molecular-level interaction of MDP with dentin components by solid-state 31P NMR spectroscopy using a light-cured commercial available MDP-based adhesive. MDP-mineral reaction/binding was confirmed in cured adhesive with dentin. Interaction with collagens needs further studies.
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Report
(5 results)
Research Products
(10 results)