自组装可以构建超分子材料
Li-Ying Wang1,2, Jian-Xiao Liang2,3, Jingyao Wang2,3
1Collaborative Innovation Centre of Regenerative Medicine and Medical BioResource Development and Application Co-constructed by the Province and Ministry, Guangxi Medical University, Nanning, Guangxi 530021, China. wanghao@nanoctr.cn.
概括
可编程自组装正在彻底改变纳米材料研究. 本综述详细介绍了序列设计,结构调节和人工智能如何为单分子检测等先进应用程序准确创建纳米结构.
科学领域:
- 超分子化学和材料科学.
- 纳米技术和生物材料工程.
背景情况:
- 体自组装可以精确控制超分子材料结构.
- 通过可编程设计,纳米材料研究正在取得进展.
研究的目的:
- 系统地审查序列设计,二次结构和动态调制在自组合中的作用.
- 探索人工智能和计算建模在设计中的应用.
- 要突出基于纳米孔的自组装纳米结构的检测应用.
主要方法:
- 关于体自组装和纳米材料制造现有文献的综述.
- 分析序列设计原理和二次结构调节 (α螺旋,β片,周期性构造).
- 对指导组装中的计算工具和人工智能的检查.
主要成果:
- 精确定义的纳米结构,如纳米管,纳米孔和纳米,可以通过受控的体自我组装来创建.
- 人工智能和计算建模促进了机制驱动的体设计,超越了经验方法.
- 基于纳米孔的系统使各种分析物的高度精确,生物相容,单分子检测成为可能.
结论:
- 为功能性超分子材料建立了一个整合序列设计,结构形成和应用的框架.
- 可编程的自我组装是开发先进纳米材料的关键策略.
- 基于的纳米结构显示出下一代生物传感技术的重大前景.
相关概念视频
Protein Complex Assembly
16.6K
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...
16.6K
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
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
Assembly of Cytoskeletal Filaments
27.1K
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...
27.1K
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


