自组装的多组件连锁体:多价值和合作性对结构和稳定性的影响
Mee-Kyung Chung1, Stephen J Lee, Marcey L Waters
1Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-3290, USA.
Journal of the American Chemical Society
|June 13, 2012
概括
这项研究使用动态组合化学来探索CH-π相互作用和键等结构元素如何影响自组装的 [2]-链的稳定性. 研究结果显示,特定的转类型是固定的,并且修改以可预测的方式影响稳定性.
科学领域:
- 超分子化学 超分子化学
- 有机化学 有机化学
- 化学热力学化学热力学
背景情况:
- 自组装 [2] - 链是一种复杂的分子架构,在各种领域都有潜在的应用.
- 了解控制它们稳定的因素对于设计和控制它们的形成至关重要.
- 之前的研究已经暗示了非共价相互作用对连锁稳定性的重要性.
研究的目的:
- 调查特定结构元素,包括CH-π相互作用,环间键和β转型,对自组装 [2] - 链的平衡稳定性的影响.
- 确定这些因素是如何在动态平衡下对 [2]-链的物种化和稳定性有所贡献的.
- 探索分子网络中多个非共价相互作用的合作效应.
主要方法:
- 动态组合化学被用来合成和研究二单体混合物.
- 单体的设计是为了系统地探测CH-π相互作用,键和β转的影响.
- 为了分析稳定性变化,进行了变异性研究和三组件动态自我组装实验.
主要成果:
- [2]-catenane的核心仅在特定位置采用II'型和VIII型β转,这些转被发现是不可修改的.
- 在CH-π-CH三明治中涉及的Aib残留物的修改显示出对稳定性的单调影响,极性异构原子是不稳定的.
- 改变关键的交环键并探索诱导效应表明,电子负替代剂和CH供体多重性增强CH-π相互作用.
结论:
- [2]-链的稳定性是由非共价相互作用的复杂相互作用决定的,形成一个合作的结合网络.
- 在这个网络的某个部分的干扰可能会导致补偿或级联的破坏稳定的效应.
- 核心β转型类型的固定性和CH-π相互作用和键的特定作用是 [2]-catenane稳定性的关键决定因素.
相关概念视频
Catenins
Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Cooperative Allosteric Transitions
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Stability of Substituted Cyclohexanes
This lesson discusses the stability of substituted cyclohexanes with a focus on energies of various conformers and the effect of 1,3-diaxial interactions.
The two chair conformations of cyclohexanes undergo rapid interconversion at room temperature. Both forms have identical energies and stabilities, each comprising equal amounts of the equilibrium mixture. Replacing a hydrogen atom with a functional group makes the two conformations energetically non-equivalent.
For example, in...
The two chair conformations of cyclohexanes undergo rapid interconversion at room temperature. Both forms have identical energies and stabilities, each comprising equal amounts of the equilibrium mixture. Replacing a hydrogen atom with a functional group makes the two conformations energetically non-equivalent.
For example, in...
Structure of Cadherins
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Chair Conformation of Cyclohexane
The chair conformation is the most stable form of cyclohexane due to the absence of angle and torsional strain. The absence of angle strain is a result of cyclohexane’s bond angle being very close to the ideal tetrahedral bond angle of 109.5° in its chair conformer. Similarly, the torsional strain is also absent owing to the perfectly staggered arrangement of bonds.
The hydrogen atoms linked to carbons are arranged in two different axial and equatorial orientations to achieve this staggered...
The hydrogen atoms linked to carbons are arranged in two different axial and equatorial orientations to achieve this staggered...
Cytoskeletal Accessory Proteins
The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...


