Binding kinetics of ultrasmall gold nanoparticles with proteins

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dc.citation.issue7
dc.citation.volume10
dc.contributor.authorLira, Andre L. [UNIFESP]
dc.contributor.authorFerreira, Rodrigo S. [UNIFESP]
dc.contributor.authorTorquato, Ricardo J. S. [UNIFESP]
dc.contributor.authorZhao, Huaying
dc.contributor.authorOliva, Maria Luiza V. [UNIFESP]
dc.contributor.authorHassan, Sergio A.
dc.contributor.authorSchuck, Peter
dc.contributor.authorSousa, Alioscka A. [UNIFESP]
dc.coverageCambridge
dc.date.accessioned2020-07-08T13:09:39Z
dc.date.available2020-07-08T13:09:39Z
dc.date.issued2018
dc.description.abstractSynthetic 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.en
dc.description.affiliationUniv Fed Sao Paulo, Dept Biochem, Sao Paulo, SP, Brazil
dc.description.affiliationNatl Inst Biomed Imaging & Bioengn, NIH, Bethesda, MD USA
dc.description.affiliationNIH, Ctr Mol Modeling, OIR, CIT, Bldg 10, Bethesda, MD 20892 USA
dc.description.affiliationUnifespUniv Fed Sao Paulo, Dept Biochem, Sao Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipSao Paulo Research Foundation
dc.description.sponsorshipNational Institute of Biomedical Imaging and Bioengineering
dc.description.sponsorshipCenter for Information Technology, National Institutes of Health, USA
dc.description.sponsorshipIDFAPESP: 2013/18481-5
dc.format.extent3235-3244
dc.identifierhttp://dx.doi.org/10.1039/c7nr06810g
dc.identifier.citationNanoscale. Cambridge, v. 10, n. 7, p. 3235-3244, 2018.
dc.identifier.doi10.1039/c7nr06810g
dc.identifier.issn2040-3364
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/54117
dc.identifier.wosWOS:000425348100015
dc.language.isoeng
dc.publisherRoyal Soc Chemistry
dc.relation.ispartofNanoscale
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.titleBinding kinetics of ultrasmall gold nanoparticles with proteinsen
dc.typeinfo:eu-repo/semantics/article
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