Molecular level evaluation on HEMA interaction with a collagen model.
Molecular level evaluation on HEMA interaction with a collagen model.
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DOI：
10.1016/j.dental.2014.11.005
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发表时间：
2015-02
期刊：
影响因子：
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通讯作者：
N. Hiraishi;N. Tochio;T. Kigawa;M. Otsuki;J. Tagami
中科院分区：
文献类型：
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作者：
N. Hiraishi;N. Tochio;T. Kigawa;M. Otsuki;J. Tagami
甲基丙烯酸羟乙酯（HEMA）在潮湿的牙本质中扩散，并在牙本质底漆和粘合过程中促进粘附。我们已经调查了分子水平之间的相互作用，HEMA和胶原蛋白模型，通过使用饱和转移差（STD）NMR.MethodsThe绑定的HEMA胶原蛋白的初步研究，通过悬浮脱矿的人牙本质粉末在4 mM的HEMA溶液1小时，并测量在分光光度计上的HEMA浓度的减少。HEMA的分子水平的相互作用与atelocollagen，这是用来作为一个胶原模型，研究了STD-NMR spectroscopy.ResultsThe HEMA浓度在悬浮液中没有改变，表明HEMA没有结合到牙本质胶原。STD-NMR证实了这一点;当去端肽胶原共振饱和时，没有饱和传播到HEMA，也没有检测到STD信号。在牙本质/粘结界面中，胶原原纤维可能被水分子包围，这阻止了直接的HEMA结合相互作用。
Objective2-Hydroxyethylmethacrylate (HEMA) diffuses in wet dentin and promotes adhesion during dentin priming and bonding. We have investigated the molecular level interaction between HEMA and a collagen model by using saturation transfer difference (STD) NMR.MethodsThe binding of HEMA to collagen was preliminarily investigated by suspending demineralized human dentin powders in a 4 mM HEMA solution for 1 h and measuring the decrease in the HEMA concentration on a spectrophotometer. The molecular level interaction of HEMA with atelocollagen, which was used as a collagen model, was investigated by STD-NMR spectroscopy.ResultsThe HEMA concentration in the suspension did not change, indicating that HEMA did not bind to dentin collagen. This was confirmed by STD-NMR; when the atelocollagen resonance was saturated, no saturation was propagated to HEMA and no STD signals were detected.SignificanceThe HEMA protons were not near the atelocollagen surface, indicating HEMA did not interact with atelocollagen. The collagen fibrils may be surrounded by water molecules in dentin/bond interfaces, which prevent the direct HEMA binding interaction.