ArticleNanoscale2018
Binding kinetics of ultrasmall gold nanoparticles with proteins.
Article in Nanoscale, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
15 citing papers in PubMed, 43 citations in OpenAlex.
- Realizing active targeting in cancer nanomedicine with ultrasmall nanoparticles.Beilstein journal of nanotechnology · 2024Review
- Functionalized GD2 Electrochemical Immunosensor to Diagnose Minimum Residual Disease of Bone Marrow in Neuroblastoma Effectively.Biosensors · 2023Article
- Aptamer-conjugated gold nanoparticles and their diagnostic and therapeutic roles in cancer.Frontiers in bioengineering and biotechnology · 2023Review
- New Paradigm for Nano-Bio Interactions: Multimolecular Assembly of a Prototypical Disordered Protein with Ultrasmall Nanoparticles.Nano letters · 2022Article
- CeOToxics · 2022Article
- Role of Ionic Strength in the Formation of Stable Supramolecular Nanoparticle-Protein Conjugates for Biosensing.International journal of molecular sciences · 2022Article
- Biomolecular interactions of ultrasmall metallic nanoparticles and nanoclusters.Nanoscale advances · 2021Review
- Analytical Methods for Characterization of Nanomaterial Surfaces.Analytical chemistry · 2021Review
- Artificial neural networks for the inverse design of nanoparticles with preferential nano-bio behaviors.The Journal of chemical physics · 2020Article
- Ultrasmall Gold Nanoparticles Coated with Zwitterionic Glutathione Monoethyl Ester: A Model Platform for the Incorporation of Functional Peptides.The journal of physical chemistry. B · 2020Article
- High Surface Reactivity and Biocompatibility of YMolecules (Basel, Switzerland) · 2020Article
- Strong dependence of the nano-bio interactions on core morphology and layer composition of ultrasmall nanostructures.The Journal of chemical physics · 2019Article
- Article
- Allosteric inhibition of α-thrombin enzymatic activity with ultrasmall gold nanoparticles.Nanoscale advances · 2019Article
- Self-adaptive multiscaling algorithm for efficient simulations of many-protein systems in crowded conditions.Physical chemistry chemical physics : PCCP · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.