球状蛋白与两性离子二氧化硅纳米颗粒相互作用的核磁共振自旋弛豫动力学

IF 15.6 1区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY
Xinyao Xiang*, Lei Bruschweiler-Li, Joseph B. Schlenoff and Rafael Brüschweiler*, 
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引用次数: 0

摘要

纳米粒子在化学和生物学各个领域的许多新兴应用需要表征纳米粒子与周围生物分子(如蛋白质)之间的相互作用。蛋白质的核磁共振自旋弛豫对与纳米粒子的相互作用高度敏感,包含了丰富的蛋白质迁移和结合动力学信息。球状蛋白与二氧化硅纳米颗粒的相互作用与脂质体纳米颗粒的相互作用明显不同,尽管两者都是由静电力驱动的。对于未修饰的二氧化硅纳米颗粒,它们与泛素等内部刚性蛋白的相互作用均匀地增加了大多数残基的主链酰胺15N横向R2弛豫。相反,对于泛素- popg脂质体相互作用,它们的横向R2谱特征表明泛素在脂质体表面进行扩散旋转运动。在这里,我们发现用磺胺甜菜碱硅氧烷两性离子分子包裹二氧化硅纳米颗粒,以一种非常类似于与脂质体观察到的相互作用模式的方式,深刻地改变了它们与蛋白质的相互作用。15N-R2弛豫表明,泛素和B-Raf的ras结合域在结合状态下都表现出垂直于纳米颗粒表面的轴向重定向运动,其中相互作用主要涉及带正电的表面区域。这些发现指出了蛋白质与具有密集带电软表面的有机或无机纳米颗粒相互作用时的整体动力学机制。这些信息可能有助于定制纳米颗粒涂层,以采用与蛋白质相互作用的特定模式,可用于控制其体内和体外功能。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Dynamics of Globular Proteins when Interacting with Zwitterionic Silica Nanoparticles by Nuclear Magnetic Resonance Spin Relaxation

Dynamics of Globular Proteins when Interacting with Zwitterionic Silica Nanoparticles by Nuclear Magnetic Resonance Spin Relaxation

The many emerging applications of nanoparticles in diverse fields in chemistry and biology require the characterization of interactions between nanoparticles and surrounding biomolecules such as proteins. Nuclear magnetic resonance spin relaxation of proteins, which is highly sensitive to interactions with nanoparticles, contains rich information about protein mobility and binding kinetics. The interactions of globular proteins with silica nanoparticles differ markedly from those with liposome nanoparticles, although both are driven by electrostatic forces. For unmodified silica nanoparticles, their interactions with an internally rigid protein like ubiquitin uniformly increase the backbone amide 15N transverse R2 relaxation for most residues. In contrast, for ubiquitin-POPG liposome interactions, their characteristic transverse R2 profiles indicate that ubiquitin undergoes diffusive rotational motions on the liposome surface. Here, we show that coating silica nanoparticles with sulfobetaine siloxane zwitterionic molecules profoundly alters their interactions with proteins in a manner that closely resembles the mode of interaction observed with liposomes. 15N-R2 relaxation reveals that ubiquitin and the Ras-binding domain of B-Raf both exhibit axial reorientational motions about an axis perpendicular to the nanoparticle surface in the bound state, where the interactions involve predominantly positively charged surface regions. These findings point toward a global dynamics mechanism of proteins when interacting with organic or inorganic nanoparticles with densely charged soft surfaces. This information may help tailor the coatings of nanoparticles to adopt specific modes of interaction with proteins that can be used to control their function in vivo and in vitro.

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来源期刊
CiteScore
24.40
自引率
6.00%
发文量
2398
审稿时长
1.6 months
期刊介绍: The flagship journal of the American Chemical Society, known as the Journal of the American Chemical Society (JACS), has been a prestigious publication since its establishment in 1879. It holds a preeminent position in the field of chemistry and related interdisciplinary sciences. JACS is committed to disseminating cutting-edge research papers, covering a wide range of topics, and encompasses approximately 19,000 pages of Articles, Communications, and Perspectives annually. With a weekly publication frequency, JACS plays a vital role in advancing the field of chemistry by providing essential research.
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