单个氨基酸修饰用于控制基于的金纳米粒子超结构
Sydney C Brooks1, Ruitao Jin2, Victoria C Zerbach1
1Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States.
Journal of the American Chemical Society
|March 13, 2023
概括
改变合物引导金纳米粒子 (Au NP) 组装成特定的螺旋超结构. 结亲和力的变化决定了从双向单的转变,影响了纳米尺度的特性.
科学领域:
- 纳米技术和材料科学
- 生物结合化学
- 计算化学
背景情况:
- 纳米粒子 (NP) 超构体根据它们的3D排列表现出新兴的特性.
- 合物有效地引导NP组合进入所需的上层结构.
- 对联体的修改可以改变纳米级结构和特性.
研究的目的:
- 调查如何改变第九个氨基酸残留在合物影响金纳米粒子 (Au NP) 螺旋组件的结构.
- 了解与黄金表面的结合亲和力和由此产生的上层结构形成之间的关系.
- 预测用于指导特定单螺旋 Au NP 超结构的新联体.
主要方法:
- 通过修改第九个氨基酸残留物来设计具有多种结合亲和力的合物.
- 用溶液化 (REST) 进行复制交换的分子动力学模拟,以评估-Au111) 表面相互作用和结合得分.
- 基于改性联体的Au NP超结构中的结构转换分析.
主要成果:
- 随着结亲和度的降低,观察到从双螺旋到单螺旋的Au NP超结构的转变.
- 一个等离子体光学信号与螺旋结构过渡同时出现.
- REST-MD模拟成功预测了用于指导单螺旋Au NP形成的新联体.
结论:
- 对前体的小修改精确地控制了纳米和微观尺度上的无机NP结构和组合.
- 基于的分子工具可以扩展到对NP超结构组装和属性的复杂控制.
- 这项工作为设计合物提供了基础,以实现目标的NP自组结果.
相关概念视频
Chirality at Nitrogen, Phosphorus, and Sulfur
5.8K
Chirality is most prevalent in carbon-based tetrahedral compounds, but this important facet of molecular symmetry extends to sp3-hybridized nitrogen, phosphorus and sulfur centers, including trivalent molecules with lone pairs. Here, the lone pair behaves as a functional group in addition to the other three substituents to form an analogous tetrahedral center that can be chiral.
A consequence of chirality is the need for enantiomeric resolution. While this is theoretically possible for all...
A consequence of chirality is the need for enantiomeric resolution. While this is theoretically possible for all...
5.8K
Chirality in Nature
13.6K
Chirality is the most intriguing yet essential facet of nature, governing life’s biochemical processes and precision. It can be observed from a snail shell pattern in a macroscopic world to an amino acid, the minutest building block of life. Most of the snails around the world have right-coiled shells because of the intrinsic chirality in their genes. All the amino acids present in the human body exist in an enantiomerically pure state, except for glycine - the sole achiral amino acid.
13.6K
Protein Folding
8.2K
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...
8.2K
Prochirality
3.9K
The concept of prochirality leads to the nomenclature of the individual faces of a molecule and plays a crucial role in the enantioselective reaction. It is a concept where two or more achiral molecules react to produce chiral products. A typical process is the reaction of an achiral ketone to generate a chiral alcohol. Here, the achiral reactant reacts with an achiral reducing agent, sodium borohydride, to generate an equimolar mixture of the chiral enantiomers of the product. For example, an...
3.9K


