Binding kinetics of ultrasmall gold nanoparticles with proteins

Binding kinetics of ultrasmall gold nanoparticles with proteins

Author Lira, Andre L. Autor UNIFESP Google Scholar
Ferreira, Rodrigo S. Autor UNIFESP Google Scholar
Torquato, Ricardo J. S. Autor UNIFESP Google Scholar
Zhao, Huaying Google Scholar
Oliva, Maria Luiza V. Autor UNIFESP Google Scholar
Hassan, Sergio A. Google Scholar
Schuck, Peter Google Scholar
Sousa, Alioscka A. Autor UNIFESP Google Scholar
Abstract 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.
xmlui.dri2xhtml.METS-1.0.item-coverage Cambridge
Language English
Sponsor Sao Paulo Research Foundation
National Institute of Biomedical Imaging and Bioengineering
Center for Information Technology, National Institutes of Health, USA
Grant number FAPESP: 2013/18481-5
Date 2018
Published in Nanoscale. Cambridge, v. 10, n. 7, p. 3235-3244, 2018.
ISSN 2040-3364 (Sherpa/Romeo, impact factor)
Publisher Royal Soc Chemistry
Extent 3235-3244
Origin http://dx.doi.org/10.1039/c7nr06810g
Access rights Closed access
Type Article
Web of Science ID WOS:000425348100015
URI https://repositorio.unifesp.br/handle/11600/54117

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