用溶剂模板折叠烯二氧化物宏循环成具有溶剂敏感光学特征的卷轴双弦绳
Peter Spenst, Ryan M Young1, Brian T Phelan1
1Department of Chemistry, Argonne-Northwestern Solar Energy Research (ANSER) Center, Northwestern University , 2145 Sheridan Road, Evanston, Illinois 60208-3113, United States.
Journal of the American Chemical Society
|January 13, 2017
概括
合成的二甲基 (PBI) 大循环表现出依赖于溶剂的折叠. 偶数PBI宏循环在芳香溶剂中形成绳状结构,可通过吸收光谱识别溶剂.
科学领域:
- 超分子化学
- 光物理学
- 有机材料科学
背景情况:
- 二胺 (PBI) 衍生物是材料科学中至关重要的染色体.
- 由于其定义的几何形状,宏观结构具有独特的特性.
- 了解PBI宏观周期中的结构-属性关系是高级应用的关键.
研究的目的:
- 合成和表征具有不同环大小 (2-9个PBI单位) 的半刚性PBI宏循环.
- 研究溶剂极性和结构对PBI宏循环构造和光物理性能的影响.
- 探索这些宏循环在溶剂传感应用中的潜力.
主要方法:
- 一个合成PBI宏循环.
- 使用光,稳定状态和短暂吸收光谱的光物理特征.
- 通过五秒刺激拉曼光谱 (FSRS) 获得详细的结构和动态见解.
- 用于溶剂特定分析的紫外线吸收光谱.
主要成果:
- PBI宏循环表现出依赖于溶剂的形状变化,在拉伸和折叠状态之间进行过渡.
- 在二甲中,拉伸的形状导致电荷分离和单片氧的形成.
- 在芳香溶剂中,均的PBI宏循环折叠成由溶剂分子模拟的绳状结构.
- 这种折叠产生了特定的激子振动合,允许从紫外线光谱中识别溶剂.
结论:
- PBI宏循环的折叠行为对周围的溶剂环境非常敏感.
- 均的PBI宏循环可以作为芳香溶剂的有效分子传感器.
- 在折叠过程中观察到的奇偶效应为设计功能性材料提供了独特的结构动机.
更多相关视频
06:55Synthesis of Cyclic Polymers and Characterization of Their Diffusive Motion in the Melt State at the Single Molecule Level
Published on: September 26, 2016
8.5K
06:16Monitoring the Effects of Illumination on the Structure of Conjugated Polymer Gels Using Neutron Scattering
Published on: December 21, 2017
6.1K
相关概念视频
Protein Folding
129.5K
Overview
129.5K
Conformations of Cyclohexane
16.6K
Cyclohexane does not exist in a planar form due to the high angle and torsional strain it would experience in the planar structure. Instead, it adopts non-planar chair and boat conformations.
The chair form is the most stable and derives its name from its resemblance to the “easy chair.” In the chair conformation, two carbon atoms are arranged out-of-plane — one above and one below, minimizing the torsional strain. In the chair form, the bond angle is very close to the ideal...
The chair form is the most stable and derives its name from its resemblance to the “easy chair.” In the chair conformation, two carbon atoms are arranged out-of-plane — one above and one below, minimizing the torsional strain. In the chair form, the bond angle is very close to the ideal...
16.6K
Molecular Chaperones and Protein Folding
20.6K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
20.6K
