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Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
Published on: April 23, 2017
纳米粒子形状的异构性决定了与表面结合的连接体的集体行为
Matthew R Jones1, Robert J Macfarlane, Andrew E Prigodich
1Department of Materials Science and Engineering, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208-3113, USA.
Journal of the American Chemical Society
|November 3, 2011
概括
黄金纳米镜中的形状异构性显著增强了连接体相互作用,与球体相比,提高了纳米粒子杂交亲和率和结合率. 这种形状驱动的效应改善了DNA和碳酸联体介导的纳米粒子组装.
科学领域:
- 纳米技术纳米技术
- 材料科学 材料科学 材料科学
- 生物结合化学 生物结合化学
背景情况:
- 纳米颗粒上的表面受限配体对于受控的组装和功能化至关重要.
- 纳米粒子的几何学可以影响连接体行为和粒子间相互作用.
- 了解形状效应是优化纳米粒子系统性能的关键.
研究的目的:
- 为了研究形状异构对纳米粒子系统中表面受限联结体特性的影响.
- 量化异型纳米颗粒与球形纳米颗粒之间的杂交亲和率和结合率的差异.
- 阐明依赖形状的连接体介导相互作用背后的机制.
主要方法:
- 三角形金纳米镜和球形金纳米颗粒与寡核酸联体的合成和功能化.
- 使用测量亲和力和关联动力学的技术,对纳米粒子杂交的表征.
- 在异型与球形纳米粒子表面的联结体介导相互作用的比较分析.
主要成果:
- 与寡核酸连接体功能化的三角形金纳米镜与球形对应物相比,显示出数百万倍更高的杂交亲和力.
- 纳米镜的关联率比球体大两倍.
- 这些增强归因于表面接触的增加,局部连接体度的增加,以及对异性质面的结构应激的减少.
结论:
- 引入形状异构性,特别是三角形金纳米镜,大大提高了表面受限联结体的性能.
- 这些发现表明,对于pH介导的关联,适用于各种联结体类型的一般原则,包括碳酸联结体.
- 形状控制的纳米粒子设计为优化纳米粒子组装和功能提供了一个强大的策略.
相关概念视频
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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...
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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...
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Molecular Shapes
Molecules have characteristic shapes that are crucial for their function. The arrangement of various electron groups around the central atom dictates their molecular geometry. Electron pairs in the valence shell of a central atom will adopt an arrangement that minimizes repulsions between the electron pairs by maximizing the distance between them. The valence electrons form either bonding pairs, located primarily between bonded atoms, or lone pairs.
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

