在受控/活激素聚合中,立体块共聚合物和战术性控制
Jean-François Lutz1, Dorota Neugebauer, Krzysztof Matyjaszewski
1Center for Macromolecular Engineering, Department of Chemistry, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania 15213, USA.
Journal of the American Chemical Society
|June 5, 2003
概括
控制的激素聚合技术,如原子转移激素聚合 (ATRP) 和可逆添加碎片转移 (RAFT) 聚合,增强了易斯酸,成功地生产了异性聚 (N,N-二甲基胺) 和立体块共聚合物.
科学领域:
- 聚合物化学 聚合物化学
- 材料科学 材料科学 材料科学
背景情况:
- 控制/活激素聚合 (CLRP) 方法对于合成具有定义架构的聚合物至关重要.
- 易斯酸可以影响聚合物战术性,影响材料性能.
- N,N-二甲基甲胺 (N,N-DMA) 聚合提供了一个研究立体化学控制的平台.
研究的目的:
- 调查ATRP,RAFT和NMP在控制多,N,N-DMA战术性的有效性.
- 探索易斯酸的使用,特别是Y ((OTf) ((3) 和Yb ((OTf) ((3),在聚合过程中增强异毒性.
- 通过激进聚合,实现第一个通过激进聚合的立体块共聚合物的单合成.
主要方法:
- 原子转移激素聚合 (ATRP) 具有特定的启动系统和CuCl/Me.
- 可逆添加碎片转移 (RAFT) 聚合利用基二硫酸转移剂.
- 氧化物介导聚合 (NMP) 使用 SG1 氧化物.
- 添加易斯酸 (Y(OTf) ((3),Yb(OTf) ((3)) 来影响聚合和战术性.
主要成果:
- 在Y的存在下,ATRP和RAFT产生了具有受控分子量,低多分散性 (<1.2) 和高同位性 (~85%的介质二) 的多N,N-DMA.
- 与易斯酸结合的NMP显示对链架构和微观结构的控制较少 (约65%的中二).
- 通过使用ATRP/Y(OTf) ((3) 和RAFT/Y(OTf) ((3) 系统,成功地证明了对抗性-b-异抗性多聚合物 (N,N-DMA) 立体块共聚合物的单合成.
结论:
- 当ATRP和RAFT聚合与Y{}OTf{}3相结合时,可以有效地控制聚{},N,N-DMA的战术性.
- 这些易斯酸介导的CLRP系统能够在单个中合成明确的立体块共聚合物.
- 这些发现为制造具有量身定制的微观结构和特性的先进聚合物材料开辟了道路.
更多相关视频
相关概念视频
Ligand Binding and Linkage
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Covalently Linked Protein Regulators
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.
Covalently Linked Protein Regulators
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.
Assembly of Signaling Complexes
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Drug-Receptor Bonds
Drug-receptor bonds are formed through various chemical forces when drugs interact with target cells. Covalent bonds, strong and irreversible, are exemplified by DNA-alkylating anticancer agents that inhibit cell division. However, such irreversible drug binding lacks selectivity and can modify the DNA of the surrounding healthy cells. Covalent binding often contributes to tissue toxicity, as seen with chloroform and paracetamol metabolites binding to the liver, causing hepatotoxicity.
In...
In...
Transducer Mechanism: Enzyme-Linked Receptors
Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Major types that are helpful drug targets include:


