Adhesion mechanisms of resin to etched dentin primed with N-methacryloyl glycine studied by 13C-NMR.

Adhesion mechanisms of resin to etched dentin primed with N-methacryloyl glycine studied by 13C-NMR.
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通过 13C-NMR 研究树脂对涂有 N-甲基丙烯酰甘氨酸底漆的蚀刻牙本质的粘附机制。

DOI:
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发表时间:
1998
期刊:
Journal of Biomedical Materials Research
影响因子:
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通讯作者:
K. Nemoto
K. Nemoto
中科院分区:
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文献类型:
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作者:
N. Nishiyama;T. Asakura;K. Suzuki;T. Sato;K. Nemoto

文献摘要

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用~(13)C-核磁共振(NMR)方法研究了树脂与N-甲基丙烯酰甘氨酸(NMGly)处理的酸蚀牙本质的pH依赖性结合强度的来源,包括自旋-晶格弛豫时间(T1)的观察。当牙本质胶原悬浮在pH = 1.6的NMGly溶液中时,归因于NMGly种类的所有碳的T1值显著降低。这表明NMGly和牙本质胶原之间存在相互作用。为了获得这种相互作用的详细信息,在胶原蛋白的模型化合物(Pro-Pro-Gly)5存在下,在pH = 1.7下测量NMGly的13 C-NMR光谱。在NMGly物质中酰胺和羧酸的羰基碳的13 C-NMR峰向更高的场移动并且T1值降低。此外,当(Pro-Pro-Gly)5与NMGly的摩尔比从1:1降低到1:3时,归因于寡肽的C-末端Gly残基中的羧酸的羰基碳的T1值显著降低。可以解释为,这表明酰胺、-NH和NMGly物质的羧酸以及寡肽的C-末端Gly残基的羧酸之间形成氢键。
The origin of the pH-dependent bond strength of the resin to etched dentin treated with N-methacryloyl glycine (NMGly) primer was studied by 13C-nuclear magnetic resonance (NMR) including spin-lattice relaxation time, T1, observation. When the dentinal collagen was suspended in the NMGly solution at pH = 1.6, the T1 values of all the carbons attributed to the NMGly species were significantly decreased. This indicated the presence of an interaction between the NMGly and the dentinal collagen. To obtain detailed information of this interaction, the 13C-NMR spectra of the NMGly were measured in the presence of the model compound for the collagen, (Pro-Pro-Gly)5 at pH = 1.7. The 13C-NMR peaks of the carbonyl carbons of the amide and carboxylic acid in the NMGly species shifted to a higher field and the T1 values decreased. Furthermore, when the molar ratio of (Pro-Pro-Gly)5 to NMGly was decreased from 1:1 to 1:3, the T1 values of the carbonyl carbon attributed to the carboxylic acid in the C-terminal Gly residue of the oligopeptide decreased dramatically. It can be construed that this indicated the formation of a hydrogen bond between the amide, -NH and the carboxylic acid of the NMGly species and the carboxylic acid of the C-terminal Gly residue of the oligopeptide.