动态螺旋β-的组装具有可切换的手性进入多种类型的金属框架
Ingyu Han1, Ha-Jin Lee2, Ilia A Guzei3
1Department of Chemistry, Yonsei University, Seoul, Republic of Korea.
Nature communications
|October 28, 2025
概括
动态螺旋式β-与银离子自组装成不同的金属框架 (MPF). 这些奇拉生物模拟材料提供可调节的孔隙环境和选择性客体识别,推进了材料科学.
科学领域:
- 超分子化学 超分子化学
- 材料科学 材料科学 材料科学
- 生物模拟化学 生物模拟化学
背景情况:
- 螺旋的金属导向组件是有前途的性仿生材料.
- 动态螺旋和它们组装成金属框架 (MPF) 尚未得到充分研究.
研究的目的:
- 为了研究12/10螺旋动态β-pentapeptides与银离子的协调驱动组件.
- 探索基于连接体性和溶剂环境的独特MPF的形成.
- 为了证明MPF孔环境的可调性,用于选择性客户识别.
主要方法:
- 合成基于碳酸酸的cis-2-aminocycloheptane β-pentapeptide配体,具有交替的性.
- 协调驱动的自组装与银离子在前离子和前离子溶剂.
- 由此产生的金属基框架的晶体分析.
- 结晶后的客人识别研究.
主要成果:
- 动态β-pentapeptides自组装成不同的MPF (Ag-1M,Ag-1P,Ag-rac-1PM),取决于溶剂和连接体的性.
- 连接物修饰允许形成模拟的MPFs与调节的孔环境.
- 一种特定的MPF (Ag-5M) 证明可以选择性地识别晶体化后的性客体.
结论:
- 动态螺旋式β-是创建多种性MPF的多功能构建块.
- 合理的体设计可以精确控制MPF孔隙环境和客结合性质.
- 这项工作为开发用于传感和分离应用的新性材料开辟了道路.
相关概念视频
Protein Folding
11.1K
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...
11.1K
Protein Folding
126.1K
Overview
126.1K
Protein Organization
155.7K
Overview
155.7K
Protein Organization
9.0K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
The primary structure of a protein is its amino acid sequence....
9.0K
Amyloid Fibrils
11.6K
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,...
11.6K
Peptide Bonds
81.9K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
81.9K


