ArticleInternational journal of molecular sciences2022
"Soft Protein Corona" as the Stabilizer of the Methionine-Coated Silver Nanoparticles in the Physiological Environment: Insights into the Mechanism of the Interaction.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- A novel fluorescent sensor based on CdTe quantum dots and DTAB-modified Au nanoparticles through aggregation-induced fluorescence recovery for the detection of l-lysine.Journal of the science of food and agriculture · 2026Article
- The protein corona at the nano-bio interface: the need for standardized methodology and opportunities for neurodegenerative disease intervention.RSC advances · 2026Review
- Selective colorimetric sensing of FeRSC advances · 2026Article
- Deciphering the formation of biogenic nanoparticles and their protein corona: State-of-the-art and analytical challenges.Analytical and bioanalytical chemistry · 2026Review
- Fungal-derived ZnO nanoparticles functionalized with riboflavin and UDP-GlcNAc exhibit potent nematicidal activity against M. incognita.Scientific reports · 2025Article
- Diatom-derived extracellular polymeric substances form eco-corona and enhance stability of silver nanoparticles.Environmental science. Nano · 2024Article
- The Effect of Sulfobetaine Coating in Inhibiting the Interaction between Lyotropic Liquid Crystalline Nanogels and Proteins.Gels (Basel, Switzerland) · 2022Article
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Authors and funding
7 authors.
Funding
Abstract
The study of the interactions between nanoparticles (NPs) and proteins has had a pivotal role in facilitating the understanding of biological effects and safe application of NPs after exposure to the physiological environment. Herein, for the first time, the interaction between L-methionine capped silver nanoparticles (AgMet), and bovine serum albumin (BSA) is investigated in order to predict the fate of AgMet after its contact with the most abundant blood transport protein. The detailed insights into the mechanism of interaction were achieved using different physicochemical techniques. The UV/Vis, TEM, and DLS were used for the characterization of the newly formed "entity", while the kinetic and thermodynamic parameters were utilized to describe the adsorption process. Additionally, the fluorescence quenching and synchronous fluorescence studies enabled the prediction of the binding affinity and gave us insight into the influence of the adsorption on the conformation state of the BSA. According to the best of our knowledge, for the first time, we show that BSA can be used as an external stabilizer agent which is able to induce the peptization of previously agglomerated AgMet. We believe that the obtained results could contribute to further improvement of AgNPs' performances as well as to the understanding of their in vivo behavior, which could contribute to their potential use in preclinical research studies.
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Registered trials
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