ArticleJournal of fluorescence2015
A Note on the use of Steady-State Fluorescence Quenching to Quantify Nanoparticle-Protein Interactions.
Article in Journal of fluorescence, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Interaction of BSA with TaMolecules (Basel, Switzerland) · 2026Article
- Mathematical Modeling for an MTT Assay in Fluorine-Containing Graphene Quantum Dots.Nanomaterials (Basel, Switzerland) · 2022Article
- Biomolecular interactions of ultrasmall metallic nanoparticles and nanoclusters.Nanoscale advances · 2021Review
- 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
- Article
- Article
- Allosteric inhibition of α-thrombin enzymatic activity with ultrasmall gold nanoparticles.Nanoscale advances · 2019Article
- Binding kinetics of ultrasmall gold nanoparticles with proteins.Nanoscale · 2018Article
- Sedimentation of Reversibly Interacting Macromolecules with Changes in Fluorescence Quantum Yield.Biophysical journal · 2017Article
Corrections and comments
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Authors and funding
1 author.
Funding
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Abstract
Steady-state fluorescence quenching is a commonly used technique to investigate the interactions between proteins and nanoparticles, providing quantitative information on binding affinity, stoichiometry and cooperativity. However, a failure to account for the limitations and pitfalls of the methodology can lead to significant errors in data analysis and interpretation. Thus, in this communication we first draw attention to a few common pitfalls in the use of fluorescence quenching to study nanoparticle-protein interactions. For example, we discuss a frequent mistake in the use of the Hill equation to determine cooperativity. We also test using both simulated and experimental data the application of a model-independent method of analysis to generate true thermodynamic nanoparticle-protein binding isotherms. This model-free approach allows for a quantitative description of the interactions independent of assumptions about the nature of the binding process [Bujalowski W, Lohman TM (1987) Biochemistry 26: 3099; Schwarz G (2000) Biophys. Chem. 86: 119].
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Registered trials
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