在多巴胺结合的DNA Aptamer 中的联体诱导折叠
Yunus A Kaiyum1, Emily Hoi Pui Chao1, Lakshmi Dhar1
1Department of Chemistry, York University, 4700 Keele St., Toronto, Ontario, M3 J 1P3, Canada.
Chembiochem : a European journal of chemical biology
|October 6, 2024
概括
DNA 体是生物传感器的关键,但它们的联体诱导结合尚不清楚. 这项研究揭示了多巴胺吸附体结构如何在结合时发生变化,影响生物传感器功能.
科学领域:
- 生物化学 生化学
- 分子生物学分子生物学
- 生物物理学的生物物理.
背景情况:
- 胺是生物传感器开发中的关键分子识别元素.
- 连接体诱导的结构形成是基于aptamer的生物传感器中常见的结合机制.
- 在体中因联体诱导的结构变化的精确机制仍然不太清楚.
研究的目的:
- 为了研究一种多巴胺结合DNA体的结合机制和体诱导的结构变化.
- 为了分析aptamer的终端干的修改如何影响多巴胺结合亲和力和结构.
- 为了将aptamer结构动力学与基于aptamer的电化学生物传感器的性能相关联.
主要方法:
- 异热定位热量计 (ITC) 用于量化结合热力学.
- 循环二重化 (CD) 光谱法用于评估结构变化.
- 核磁共振 (NMR) 光谱 (1H NMR) 探测结构动力学和识别连接体诱导的变化.
- 系统地修改体的终端茎长度.
主要成果:
- 所有研究的阿普坦体都通过具有不利的输热驱动过程与多巴胺结合.
- 观察到结合亲和力下降,因为体的终端干长度缩短了.
- 干结合诱导了体中新结构的形成,由1H NMR信号证明.
- 只有当结构形成区域靠近传感器表面时,才能实现功能性的电化学aptamer-based生物传感器.
结论:
- 终端茎的长度显著影响多巴胺DNA吸附体的结合亲和力.
- 带结合会诱导DNA吸收体中的特定结构重组.
- 体结构形成区域与传感器表面的接近对于开发功能性的基于体的电化学生物传感器至关重要.
相关概念视频
Ligand Binding Sites
12.8K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
12.8K
Conserved Binding Sites
4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K
Molecular Chaperones and Protein Folding
17.8K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
17.8K
Ligand Binding and Linkage
4.8K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.8K


