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Controlling the surface functionalization of ultrasmall gold nanoparticles by sequence-defined macromolecules.
Chemistry - A European Journal ( IF 3.9 ) Pub Date : 2020-09-22 , DOI: 10.1002/chem.202003804
Selina Beatrice van der Meer 1 , Theresa Seiler 2 , Christin Buchmann 2 , Georgia Partalidou 2 , Sophia Boden 2 , Kateryna Loza 1 , Marc Heggen 3 , Jürgen Linders 4 , Oleg Prymak 1 , Cristiano L P Oliveira 5 , Laura Hartmann 2 , Matthias Epple 1
Affiliation  

Ultrasmall gold nanoparticles (diameter about 2 nm) were surface‐functionalized with cysteine‐carrying precision macromolecules. These consisted of sequence‐defined oligo(amidoamine)s (OAAs) with either two or six cysteine molecules for binding to the gold surface and either with or without a PEG chain (3400 Da). They were characterized by 1H NMR spectroscopy, 1H NMR diffusion‐ordered spectroscopy (DOSY), small‐angle X‐ray scattering (SAXS), and high‐resolution transmission electron microscopy. The number of precision macromolecules per nanoparticle was determined after fluorescent labeling by UV spectroscopy and also by quantitative 1H NMR spectroscopy. Each nanoparticle carried between 40 and 100 OAA ligands, depending on the number of cysteine units per OAA. The footprint of each ligand was about 0.074 nm2 per cysteine molecule. OAAs are well suited to stabilize ultrasmall gold nanoparticles by selective surface conjugation and can be used to selectively cover their surface. The presence of the PEG chain considerably increased the hydrodynamic diameter of both dissolved macromolecules and macromolecule‐conjugated gold nanoparticles.

中文翻译:

通过序列定义的大分子控制超小金纳米颗粒的表面功能化。

超小型金纳米颗粒(直径约 2 nm)通过携带半胱氨酸的精密大分子进行表面功能化。它们由序列定义的寡聚(酰氨基胺)(OAA)组成,具有两个或六个半胱氨酸分子,用于结合到金表面,并且带有或不带有 PEG 链(3400 Da)。通过1 H NMR 光谱、1 H NMR 扩散有序光谱 (DOSY)、小角 X 射线散射 (SAXS) 和高分辨率透射电子显微镜对其进行了表征。每个纳米颗粒的精密大分子数量在荧光标记后通过紫外光谱以及定量1 H NMR 光谱测定。每个纳米颗粒携带 40 到 100 个 OAA 配体,具体取决于每个 OAA 的半胱氨酸单元数量。每个配体的足迹约为每个半胱氨酸分子0.074 nm 2。OAA 非常适合通过选择性表面共轭来稳定超小型金纳米颗粒,并可用于选择性覆盖其表面。PEG链的存在显着增加了溶解的大分子和大分子共轭金纳米颗粒的流体动力学直径。
更新日期:2020-09-22
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