Binding kinetics of ultrasmall gold nanoparticles with proteins
| Autor: | Huaying Zhao, Rodrigo da Silva Ferreira, Alioscka A. Sousa, Peter Schuck, Sergio A. Hassan, Ricardo J.S. Torquato, Maria Luiza Vilela Oliva, André L. Lira |
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| Rok vydání: | 2018 |
| Předmět: |
Chemistry
Kinetics Rational design Metal Nanoparticles Nanoparticle Protein Corona 02 engineering and technology Buffer solution 010402 general chemistry 021001 nanoscience & nanotechnology 01 natural sciences Article Receptor–ligand kinetics 0104 chemical sciences chemistry.chemical_compound Colloidal gold Biophysics General Materials Science Gold 0210 nano-technology Protein Binding Macromolecule |
| Zdroj: | Nanoscale. 10:3235-3244 |
| ISSN: | 2040-3372 2040-3364 |
| Popis: | Synthetic ultrasmall nanoparticles (NPs) can be designed to interact with biologically active proteins in a controlled manner. However, the rational design of NPs requires a clear understanding of their interactions with proteins and the precise molecular mechanisms that lead to association/dissociation in biological media. Although much effort has been devoted to the study of the kinetics mechanism of protein corona formation on large NPs, the nature of NP-protein interactions in the ultrasmall regime is radically different and poorly understood. Using a combination of experimental and computational approaches, we studied the interactions of a model protein, CrataBL, with ultrasmall gold NPs passivated with p-mercaptobenzoic acid (AuMBA) and glutathione (AuGSH). We have identified this system as an ideal in vitro platform to understand the dependence of binding affinity and kinetics on NP surface chemistry. We found that the structural and chemical complexity of the passivating NP layer leads to quite different association kinetics, from slow and reaction-limited (AuGSH) to fast and diffusion-limited (AuMBA). We also found that the otherwise weak and slow AuGSH-protein interactions measured in buffer solution are enhanced in macromolecular crowded solutions. These findings advance our mechanistic understanding of biomimetic NP-protein interactions in the ultrasmall regime and have implications for the design and use of NPs in the crowded conditions common to all biological media. |
| Databáze: | OpenAIRE |
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