循环组件的动态控制以形成更高阶组件
Chongyang Wu1, Hongyue Zhang1, Nan Kong1
1Key Laboratory of Precise Synthesis of Functional Molecules of Zhejiang Province, Department of Chemistry, School of Science, Westlake University, Institute of Natural Sciences, Westlake Institute for Advanced Study, No. 600 Dunyu Road, Hangzhou, 310024, Zhejiang Province, China.
Angewandte Chemie (International ed. in English)
|July 6, 2023
概括
研究人员设计了一种交替的D,L,模仿自然性逆转并形成独特的交织的纳米结构. 这种生物材料平台推进了功能性生物材料和催化剂.
科学领域:
- 超分子化学 超分子化学
- 生物材料科学 生物材料科学
- 有机化学 有机化学
背景情况:
- 奇拉性,不对称性,环链对称性和等级组合是具有重大生物影响的基本自然现象.
- 在人工系统中研究这些复杂的行为是具有挑战性的,因为复制自然特征的困难.
- 了解这些现象对于开发先进的功能材料至关重要.
研究的目的:
- 设计和验证一个人工系统,在循环化之前重现自然性逆转.
- 在一个新的类系统中研究环链复合性,热稳定性和动态组装.
- 探索合理设计的在模仿生物材料开发的自然现象的潜力.
主要方法:
- 在水中自组装的交替D,L的设计.
- 形成一个不对称的循环含有4-imidazolidinone环.
- 对纳米结构形成的分析,包括性和组装行为.
主要成果:
- 在水性环境中成功复制自然性逆转和循环.
- 由4-imidazolidinone环驱动的独特,交织的纳米结构的形成.
- 在纳米结构中证实左撇子,证明了奇拉性诱导的自我组装.
结论:
- 理性设计的可以有效地模仿复杂的自然现象,如性逆转和双相.
- 开发的体系统作为研究超分子组合和开发功能生物材料的平台.
- 这项研究为创造新型催化剂,抗生素和先进超级分子开辟了道路.
相关概念视频
Protein Complex Assembly
10.7K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.7K
Assembly of Cytoskeletal Filaments
21.1K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
21.1K
Protein Folding
8.1K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.1K
Formation of Higher-order Actin Filaments
3.0K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
The high-order actin...
3.0K
Assembly of Signaling Complexes
5.8K
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,...
5.8K
Protein Organization
138.6K
Overview
138.6K


