Interaction between Demineralized Dentin and HEMA
| Project/Area Number |
11671955
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
補綴理工系歯学
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| Research Institution | Nihon University |
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Principal Investigator |
NORIHIRO Nishiyama Nihon University, School of Dentistry at Matsudo, Associate Professor, 松戸歯学部, 助教授 (90112953)
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| Project Period (FY) |
1999 – 2000
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| Project Status |
Completed (Fiscal Year 2000)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2000: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1999: ¥3,200,000 (Direct Cost: ¥3,200,000)
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| Keywords | Dentin adhesion / Adhesion mechanism / HEMA / Adsorption characteristics / NMR / 脱灰象牙質 / 象牙質コラーゲン / ^<13>C NMR / 縦緩和時間 / 相互作用 |
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| Research Abstract |
Previously, we had reported that the carbonyl group of the ester portion in the HEMA molecule interacted with the dentinal collagen. In this study, in order to identify the collagen function where the carbonyl group in the HEMA molecule adsorbed, the details of the interaction between HEMA and oligopeptide were investigated by using the ^<13>C NMR technique.
The oligopeptide used as a model compound for the collagen consists of Pro-Hyp-Gly-Pro-Arg-Gly-Pro-Asp-Gly. The oligopeptide and the HEMA were dissolved into 0.600 g of 20 mass% D_2O solution. The ^<13>C NMR spin-lattice relaxation time, T_1, observation of the carbons attributed to the HEMA and the oligopeptide was conducted both alone and in the presence of them using an EX270 spectrometer (JEOL).
The addition of the oligopeptide to the HEMA solution resulted in a decrease in the T_1 value of the carbons assigned to the HEMA molecule. The degree of the decrease in the T_1 value of the carbons was dependent upon the types of carbon nuclei. When the pH value of the oligopeptide solution was decreased, the T^1 value of the carbonyl carbon in the HEMA molecule decreased. Which reflecting the decrease in the T_1 value of the carbonyl carbons attributed to the carboxylic acid group of the side chain of the Asp and the C-terminal Gly in the oligopeptide molecule.
We conclude that the carbonyl group in the HEMA molecule would form a hydrogen bonded interaction with the carboxylic acid group of the side chain of the amino acid residue in the dentinal collagen macromolecule.
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Report
(3 results)
Research Products
(3 results)
