金属二甲基胺复合物的前所未有的双光切换反应
Amir Aliyan1, Benjamin Kirby1, Christopher Pennington1
1Departments of Chemistry, ‡Bioengineering, §Materials Science & Nanoengineering, and #Shared Equipment Authority, Rice University , Houston, Texas 77005, United States.
Journal of the American Chemical Society
|July 8, 2016
概括
这项研究引入了一种用于监测粉样β (Aβ) 蛋白聚合的新型探针. 复合物[Re ((CO) 3 ((dppz)) ((Py)))) 呈现出显著的光发光度增加,使得Aβ的实时跟踪成为可能.
科学领域:
- 生物物理化学
- 材料科学
- 神经科学
背景情况:
- 蛋白质聚合,特别是粉样β (Aβ),是神经退行性疾病的核心.
- 开发用于监测蛋白质聚合的敏感探针对于了解疾病机制和药物发现至关重要.
- 光物理探测器提供了对聚合过程的动态见解.
研究的目的:
- 报告一种新型金属二氧化复合物的光发光反应, [Re(CO) 3(dppz) ((Py) ](+),对聚合的Aβ.
- 展示该探针对Aβ聚合的实时监测的实用性.
- 在纤维状Aβ的存在下研究探针的独特光切换特性.
主要方法:
- 复合物的合成和特征 [Re(CO) 3(dppz) ((Py) ] ((+).
- 探测器对聚合Aβ的光发光的光谱分析.
- 使用探测器的光切换行为实时监测Aβ聚合.
- 光物理研究包括在362nm激发二次光切换.
主要成果:
- 在与纤维状Aβ (主光切换) 相互作用时,复合体[Re ((CO) 3 ((dppz)) ((Py)))) 显示光发光的立即增加.
- 在362nm光照射下进一步增强光发效应,观察到前所未有的二次光切换效应.
- 实现了光发光的总增加105倍,提供了高度敏感的信号.
- 探测器有效地实时监测了Aβ聚合.
结论:
- 复合物[Re ((CO) 3 ((dppz)) ((Py)) ] ((+)) 作为检测聚合氨基β的高度敏感和响应的探针.
- 双光切换机制为蛋白质聚合的定量监测提供了一种新方法.
- 这种探测器对蛋白质聚合的基础研究和神经退行性疾病研究中的高通量药物查具有重大潜力.
相关概念视频
03:02Colors and Magnetism
14.5K
Color in Coordination Complexes
When atoms or molecules absorb light at the proper frequency, their electrons are excited to higher-energy orbitals. For many main group atoms and molecules, the absorbed photons are in the ultraviolet range of the electromagnetic spectrum, which cannot be detected by the human eye. For coordination compounds, the energy difference between the d orbitals often allows photons in the visible range to be absorbed and emitted, which is seen as colors by the human...
When atoms or molecules absorb light at the proper frequency, their electrons are excited to higher-energy orbitals. For many main group atoms and molecules, the absorbed photons are in the ultraviolet range of the electromagnetic spectrum, which cannot be detected by the human eye. For coordination compounds, the energy difference between the d orbitals often allows photons in the visible range to be absorbed and emitted, which is seen as colors by the human...
14.5K
03:03Amyloid Fibrils
12.8K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
12.8K