A peptide topological template for the dispersion of [60]fullerene in water

Bartocci, Silvia; Mazzier, Daniela; Moretto, Alessandro; Mba, Miriam

doi:10.1039/c4ob02102a

Cited by 9 publications

(4 citation statements)

References 32 publications

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“…As indicated by references cited herein, non-specific aqueous dispersion of fullerenes by proteins and protein interactions with nanotubes have been previously reported, and more recent reports show that this can also be achieved by appropriately-designed peptides [28] . In the work we have presented here, we have shown how it can be possible to take advantage of the specific structural and functional properties of natural surfactant proteins (such as latherin and Rsn-2) to effect solubilization and interaction with fullerenes and related materials, avoiding more aggressive sonication or chemical modification techniques that have been employed elsewhere (see [29] , [30] for recent examples).…”

Section: Resultsmentioning

confidence: 57%

Aqueous solubilization of C60 fullerene by natural protein surfactants, latherin and ranaspumin-2

Vance

Desai

Smith

et al. 2016

Biophysical Chemistry

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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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Section: Resultsmentioning

confidence: 57%

Aqueous solubilization of C60 fullerene by natural protein surfactants, latherin and ranaspumin-2

Vance

Desai

Smith

et al. 2016

Biophysical Chemistry

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“…A poly disulfide sheet is the best way to force repulsive residues into a "β-carpet" at pH values where they are entirely charged. In addition to obvious antimicrobial (membrane disruptive) applications (as per the related but synthetically problematic θ-defensin 13,14 ), this class of amphipathic peptides could be useful for catalysis, 41 metal binding, or selective detergents 42 and already resembles a common hydrogel-forming structure consisting of alternating valine/lysine. 43−48 Structurally rigid β-sheets with central disulfides have a range of other potential applications, such as minimalist scaffolds for pharmacophore display, rigid spacers, and building blocks for more complex structures.…”

Section: ■ Discussionmentioning

confidence: 99%

“…A poly disulfide sheet is the best way to force repulsive residues into a “β-carpet” at pH values where they are entirely charged. In addition to obvious antimicrobial (membrane disruptive) applications (as per the related but synthetically problematic θ-defensin , ), this class of amphipathic peptides could be useful for catalysis, metal binding, or selective detergents and already resembles a common hydrogel-forming structure consisting of alternating valine/lysine. − …”

Section: Discussionmentioning

confidence: 99%

Disulfide-Mediated β-Strand Dimers: Hyperstable β-Sheets Lacking Tertiary Interactions and Turns

2015

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Disulfide bonds between cysteine residues are essential to the structure and folding of many proteins. Yet their role in the design of structured peptides and proteins has frequently been limited to use as intrachain covalent staples that reinforce existing structure or induce knot-like conformations. In β-hairpins, their placement at non-H-bonding positions across antiparallel strands has proven useful for achieving fully folded positive controls. Here we report a new class of designed β-sheet peptide dimers with strand-central disulfides as a key element. We have found that the mere presence of a disulfide bond near the middle of a short peptide chain is sufficient to nucleate some antiparallel β-sheet structure; addition of β-capping units and other favorable cross-strand interactions yield hyperstable sheets. Strand-central cystines were found to be superior to the best designed reversing turns in terms of nucleating β-sheet structure formation. We have explored the limitations and possibilities of this technique (the use of disulfides as sheet nucleators), and we provide a set of rules and rationales for the application and further design of disulfide-tethered "turnless" βsheets.

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“…A cyclic, hydrogel-forming decapeptide can been used to solubilize fullerene by means of ultra-high vibration ball milling, thus obtaining a water-soluble nanocomposite based on π-π interactions. Despite the fact that this complex changes the gelation properties of the peptide, since in the presence of C 60 precipitation occurs, the proposed approach results to be very useful to prepare colloidal dispersions for biomedical uses [27].…”

Section: Polypeptide Hydrogelsmentioning

confidence: 99%

The Glitter of Carbon Nanostructures in Hybrid/Composite Hydrogels for Medicinal Use

Iglesias¹,

Bosi²,

Melchionna³

et al. 2016

CTMC

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In recent years, we have witnessed to fast developments in the medicinal field of hydrogels containing various forms of integrated nanostructured carbon that adds interesting mechanical, thermal, and electronic properties. Besides key advances in tissue engineering (especially for conductive tissue, such as for the brain and the heart), there has been innovation also in the area of drug delivery on-demand, with engineered hydrogels capable of repeated response to light, thermal, or electric stimuli. This mini-review focusses on the most promising developments as applied to the gelation of protein/ peptide (including self-assembling amino acids and low-molecular-weight gelators), polysaccharide, and/or synthetic polymer components in medicine. The emerging field of graphene-only hydrogels is also briefly discussed, to give the reader a full flavor of the rising new paradigms in medicine that are made possible through the integration of nanostructured carbon (e.g., carbon nanotubes, nanohorns, nanodiamonds, fullerene, etc.). Nanocarbons are offering great opportunities to bring on a revolution in therapy that the modern medicinal chemist needs to master, to realise their full potential into powerful therapeutic solutions for the patient.

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A peptide topological template for the dispersion of [60]fullerene in water

Cited by 9 publications

References 32 publications

Aqueous solubilization of C60 fullerene by natural protein surfactants, latherin and ranaspumin-2

Aqueous solubilization of C60 fullerene by natural protein surfactants, latherin and ranaspumin-2

Disulfide-Mediated β-Strand Dimers: Hyperstable β-Sheets Lacking Tertiary Interactions and Turns

The Glitter of Carbon Nanostructures in Hybrid/Composite Hydrogels for Medicinal Use

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