Raman Project Center for Medical and Biological Applications, Shimane University, 1060 Nishikawatsu, Matsue, Shimane 690-8504, Japan.
Faculty of Life and Environmental Sciences, Shimane University, 1060 Nishikawatsu, Matsue, Shimane 690-8504, Japan.
Anal Chem. 2020 Jun 16;92(12):8133-8141. doi: 10.1021/acs.analchem.0c00076. Epub 2020 May 14.
We explored the influence of embryonic bioactivity on the water structure using near-infrared (NIR) spectroscopy and imaging. Four groups of Japanese medaka fish () eggs were studied: (a) one group of eggs was activated by fertilization, and (b-d) three groups of eggs were not activated because embryogenesis was stopped or not started by (b) culturing under cold temperature, (c) instant freezing, or (d) lack of fertilization. The yolks of the activated eggs contained higher proportions of weakly hydrogen bonded water than those of nonactivated eggs. A possible factor responsible for the significant changes in the water structure was revealed to be a protein secondary structural change from an α-helix to a β-sheet in the activated eggs. NIR images of the activated eggs successfully visualized the water structural variation in the yolk with a higher proportion of weak hydrogen bonds due to the activation of embryonic development. The embryogenic activity could be assessed through the water hydrogen bond network, which is affected by newly generated proteins with different secondary structures.
我们使用近红外（NIR）光谱和成像技术探索了胚胎生物活性对水结构的影响。研究了四组日本青鳉鱼（）卵：（a）一组卵通过受精激活，（b-d）三组卵未激活，因为胚胎发生分别通过（b）在低温下培养、（c）即时冷冻或（d）缺乏受精而停止或未开始。激活卵的蛋黄中含有较高比例的弱氢键水，而非激活卵则没有。导致水结构发生显著变化的一个可能因素被揭示为激活卵中蛋白质二级结构从α-螺旋向β-折叠的变化。激活卵的 NIR 图像成功地可视化了由于胚胎发育激活而导致的蛋黄中弱氢键比例较高的水结构变化。通过水氢键网络可以评估胚胎发生活性，该网络受具有不同二级结构的新生成蛋白质的影响。
