联合组装调节纤维的催化活动
Albin Lahu1, Shao-Lin Wu1, Maximilian Schuler1,2
1Max Planck Institute for Polymer Research, Ackermannweg 10, D-55128, Mainz, Germany.
Angewandte Chemie (International ed. in English)
|December 5, 2025
概括
研究人员设计了可以自组装成纤维的催化剂,从而获得反-酶活性. 与其他一起组装精确地控制了这种催化活性,推进了基于的催化.
科学领域:
- 超分子化学 超分子化学
- 催化剂是一种催化剂.
- 生物材料是一种生物材料.
背景情况:
- 序列自组装成超分子结构.
- 这些结构为催化化学反应创造了微环境.
- 通过联合组装设计催化微环境尚未得到充分探索.
研究的目的:
- 在自我组装时引入具有逆酶活性的序列.
- 研究联合组装策略来设计催化微环境.
- 通过异质的超分子组合调节催化活性.
主要方法:
- 通过合成变异优化序列以检测逆酶活性.
- 具有特征的质结构形成特性.
- 使用与非活性的联合组合来调整催化功能.
主要成果:
- 在自我组装的纤维中实现了逆酶活性.
- 通过联合组装证明了催化活性的动态上下调节.
- 观察到带有正电荷的联合组件活动增加,带有负电荷的联合组件活动减少.
结论:
- 合组装是一种可行的策略,用于设计催化微环境.
- 异质的超分子组合可以精确控制催化剂活性.
- 这项工作推进了基于的催化剂领域.
相关概念视频
Protein Folding
10.9K
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...
10.9K
Protein Folding
125.8K
Overview
125.8K
Amyloid Fibrils
11.5K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
11.5K
Protein Complex Assembly
16.5K
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...
16.5K
Assembly of Cytoskeletal Filaments
27.0K
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...
27.0K
Allosteric Proteins-ATCase
6.4K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
6.4K


