Control of interface between tooth tissue and resin by amino acid derivative

将牙齿修补程序和粘合剂应用结合起来的技术已经开发出来，以便在一个广域应用程序中实现Caries的功能重建。好吧，这很难形成完美的束缚，一个良好的边缘缺口闭合、束缚强度和耐久性，在一种严重的胸部条件下。主要的问题是在牙齿修补和修补之间的界面层的形成和物理性质上。因此，我们综合了氨基酸衍生物（NMωA），其中一种化学化合物具有亲和力，特别是通过研究与牙科聚合物的相互作用。在本研究中，按顺序确定了聚合功能组之间的相互作用的NMωA形式，聚合化学模型中NMωA的放松时间，该组合是imino单元和羧基单元的最后部分，即测量了^<13>CNMR （T_1）的测量也随之而来。10%的寡肽（5根脯氨酸，蛋白质/氨基酸单位） ... More 在hydrochloric acid added deuterium oxide aqueous solution中溶解。该解决方案是在pH值为1.7时制造的。在同源化后，0.6克这种寡肽的问题解决方案被放置在核磁共振样品管中。6.73×105或20.19 × 10^5摩尔的NMωA作为NMR样品使用。T_1使用EX 270 MHz光谱仪进行了测量（Nihon Denshi），在25℃的温度下，用180 °-τ-90 °脉冲序列进行了表征。寡肽在NM ω A的均匀溶液中具有共存性，根据顺序进行测试，在NM ωA的分子中，酰胺单元和碳单元的相互作用，碳基碳的T_1的价值与这些功能组相似，因为它们与退化牙齿中的共存者相似。与非共存的链条相比，这是一个巨大的衰退。从上面的结果来看，在NMωA的分子中展示了侧链碳单元和氢键在聚合物中形成的侧链的功能组。Furthermore，在羟基苯甲酸酯（HEMA）的情况下，它被确认为在相同肽和分子中的碳基单元之间存在强烈的相互作用。Less（低）

The bonding technique to tooth tissue including etching procedure and adhesive application was developed to get functional reconstruction of the caries in a wide area application. However, it is difficult to make a perfect bonding, a good characteristic of marginal gap closure, bonding strength and durability under a severe condition of buccal cavity. The main problem is on the formation and the physical properties of the interface layer between tooth tissue and resin. Therefore, we synthesize the amino acid derivative (NMωA) which has chemical compound affinity, especially by examining the interaction with dentinal collagen. In this study, in order to specify the NMωA formed by the interaction of collagen functional group, the relaxation time of NMωA in the collagen model chemical, compound that has an end part of imino unit and carboxyl unit was measured.The measurement of ^<13>CNMR (T_1) is as follows. Oligopeptide of 10% (5 bodies of prolylprolylglycine, unit of protein/amino acid) … More were dissolved in hydrochloric acid added deuterium oxide aqueous solution. The aqueous solution was manufactured at the pH of 1.7. After homogenized, 0.6g of this oligopeptide aqueous solution was placed in the NMR sample tube. 6.73×105 or 20.19 x 10^5 mol of NMωA was used as the NMR sample. T_1 was measured using an EX270MHz spectrometer (Nihon Denshi), which is performed with 180゜-τ-90゜ pulse sequence, in the temperature of 25℃.As oligopeptides were coexist in NMωA aqueous solution, in order to examine an interaction of amide unit and carbonyl unit in the molecule of NMωA with the oligopeptide, the value of T_1 of carbonyl carbon which revert to these functional groups was similar to that was coexists in the deashing dentine. Compared to that of the non-coexistence chain, there was a great decrease. From the above result, the presents of amide and carboxyl unit in the molecule of NMωA showed that the side chains functional group of carbonyl unit and hydrogen bond in the collagen are formed. Furthermore, in case of hydroxymethacrylate (HEMA), it was identified that there was a strong interaction between the carbonyl unit in the same peptide and the carbonyl unit in the molecule. Less