ArticleBiophysical chemistry
Aqueous solubilization of C60 fullerene by natural protein surfactants, latherin and ranaspumin-2.
Article in Biophysical chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 29 citations in OpenAlex.
- Interaction between pristine nCFrontiers in bioengineering and biotechnology · 2025Article
- A Quantum Mechanical MP2 Study of the Electronic Effect of Nonplanarity on the Carbon Pyramidalization of Fullerene CNanomaterials (Basel, Switzerland) · 2024Article
- Enhanced Uptake and Phototoxicity of CNanomaterials (Basel, Switzerland) · 2022Article
- Dissecting the Supramolecular Dispersion of Fullerenes by Proteins/Peptides: Amino Acid Ranking and Driving Forces for Binding to CInternational journal of molecular sciences · 2021Article
- Pristine CNeurochemical research · 2020Article
- Adsorptive Removal of Antibiotic Ciprofloxacin from Aqueous Solution Using Protein-Modified Nanosilica.Polymers · 2020Article
- Preparation and photo-induced activities of water-soluble amyloid β-CRSC advances · 2018Article
- CMaterials (Basel, Switzerland) · 2018Article
- Frog foams and natural protein surfactants.Colloids and surfaces. A, Physicochemical and engineering aspects · 2017Article
- Fullerenes in Biology and Medicine.Journal of materials chemistry. B · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
C60 fullerene is not soluble in water and dispersion usually requires organic solvents, sonication or vigorous mechanical mixing. However, we show here that mixing of pristine C60 in water with natural surfactant proteins latherin and ranaspumin-2 (Rsn-2) at low concentrations yields stable aqueous dispersions with spectroscopic properties similar to those previously obtained by more vigorous methods. Particle sizes are significantly smaller than those achieved by mechanical dispersion alone, and concentrations are compatible with clusters approximating 1:1 protein:C60 stoichiometry. These proteins can also be adsorbed onto more intractable carbon nanotubes. This promises to be a convenient way to interface a range of hydrophobic nanoparticles and related materials with biological macromolecules, with potential to exploit the versatility of recombinant protein engineering in the development of nano-bio interface devices. It also has potential consequences for toxicological aspects of these and similar nanoparticles.
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Registered trials
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