共价后组装修改触发波罗姆环的结构变化
Wen-Xi Gao1, Hui-Jun Feng1, Yue-Jian Lin1
1Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, State Key Laboratory of Molecular Engineering of Polymers, Department of Chemistry , Fudan University , Shanghai 200433 , P. R. China.
Journal of the American Chemical Society
|May 24, 2019
概括
研究人员使用连接物交换和迪尔斯-阿尔德反应演示了新的超分子转化级联. 这些反应可以通过触发的拓变化来控制波罗密环的结合,解结合和修改.
科学领域:
- 超分子化学
- 有机化学
- 材料科学
背景情况:
- 波罗姆环 (BR) 是具有独特拓性质的复杂互锁结构.
- 控制超分子结构的组装和拆卸对于开发先进材料至关重要.
研究的目的:
- 开发一种新的无模板,四边形波罗密环 (BR).
- 调查这些BR的度依赖的连接和解接机制.
- 通过反向电子需求迪尔斯-阿尔德尔 (IEDDA) 反应进行组装后修改来探索超分子结构变化.
主要方法:
- 用于BR构造的连接物交换反应.
- 对BR的度依赖的结合和解结合的观察.
- 用于触发转换的逆电子需求迪尔斯-阿尔德反应 (IEDDA).
主要成果:
- 成功合成了没有模板的四边缘BRs.
- 证明了对BR连接和解接的度依赖控制.
- 通过IEDDA反应实现了波罗姆前体的组装后修饰.
- 由IEDDA反应引起的受控拓变化,包括解结.
结论:
- 超分子转换级联为构建和操纵复杂架构提供了多功能平台.
- IEDDA反应提供了一个强大的工具来触发波罗姆环系统的拓变化和组装后修改.
- 开发的系统可以通过外部刺激来精确控制超分子拓.
相关概念视频
Covalent Bonding and Lewis Structures
60.9K
Compared to ionic bonds, which results from the transfer of electrons between metallic and nonmetallic atoms, covalent bonds result from the mutual attraction of atoms for a “shared” pair of electrons.
60.9K
Covalently Linked Protein Regulators
8.9K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
8.9K
Network Covalent Solids
16.1K
Network covalent solids contain a three-dimensional network of covalently bonded atoms as found in the crystal structures of nonmetals like diamond, graphite, silicon, and some covalent compounds, such as silicon dioxide (sand) and silicon carbide (carborundum, the abrasive on sandpaper). Many minerals have networks of covalent bonds.
To break or to melt a covalent network solid, covalent bonds must be broken. Because covalent bonds are relatively strong, covalent network solids are typically...
To break or to melt a covalent network solid, covalent bonds must be broken. Because covalent bonds are relatively strong, covalent network solids are typically...
16.1K
Covalent Bonds
160.7K
Overview
160.7K
Covalent Bonds
10.2K
Overview
When two atoms share electrons to complete their valence shells, they create a covalent bond. An atom's electronegativity—the force with which shared electrons are pulled towards an atom—determines how the electrons are shared. Molecules formed with covalent bonds can be either polar or nonpolar. Atoms with similar electronegativities form nonpolar covalent bonds; the electrons are shared equally. Atoms with different electronegativities share electrons unequally,...
When two atoms share electrons to complete their valence shells, they create a covalent bond. An atom's electronegativity—the force with which shared electrons are pulled towards an atom—determines how the electrons are shared. Molecules formed with covalent bonds can be either polar or nonpolar. Atoms with similar electronegativities form nonpolar covalent bonds; the electrons are shared equally. Atoms with different electronegativities share electrons unequally,...
10.2K
Histone Modification
16.0K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
16.0K


