Montellano Alejandro, Ros Tatiana Da, Bianco Alberto, Prato Maurizio
Fullerene C₆₀ as a multifunctional system for drug and gene delivery Article de journal
Dans: Nanoscale, vol. 3, no. 10, p. 4035–4041, 2011, ISSN: 2040-3372.
Résumé | Liens | BibTeX | Étiquettes: DNA, Drug Carriers, Fullerenes, Gene Transfer Techniques, I2CT, Immunoconjugates, Plasmids, Team-Bianco
@article{montellano_fullerene_2011,
title = {Fullerene C₆₀ as a multifunctional system for drug and gene delivery},
author = {Alejandro Montellano and Tatiana Da Ros and Alberto Bianco and Maurizio Prato},
doi = {10.1039/c1nr10783f},
issn = {2040-3372},
year = {2011},
date = {2011-10-01},
journal = {Nanoscale},
volume = {3},
number = {10},
pages = {4035--4041},
abstract = {The fullerene family, and especially C(60), has delighted the scientific community during the last 25 years with perspective applications in a wide variety of fields, including the biological and the biomedical domains. Several biomedical uses have been explored using water-soluble C(60)-derivatives. However, the employment of fullerenes for drug delivery is still at an early stage of development. The design and synthesis of multifunctionalized and multimodal C(60) systems able to cross the cell membranes and efficiently deliver active molecules is an attracting challenge that involves multidisciplinary strategies. Promising results have emerged in the last years, bringing fullerenes again to the front of interest. Herein, the state of the art of this emerging field is presented and illustrated with some of the most representative examples.},
keywords = {DNA, Drug Carriers, Fullerenes, Gene Transfer Techniques, I2CT, Immunoconjugates, Plasmids, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Zacchigna Marina, Klumpp Cedric, Prato Maurizio, Bianco Alberto
In vitro behavior of multifunctionalized fullerene-warfarin conjugates Article de journal
Dans: Journal of Nanoscience and Nanotechnology, vol. 9, no. 10, p. 6210–6221, 2009, ISSN: 1533-4880.
Résumé | Liens | BibTeX | Étiquettes: Animals, Anticoagulants, Fullerenes, I2CT, In Vitro Techniques, Mice, Spectrophotometry, Team-Bianco, Ultraviolet, Warfarin
@article{zacchigna_vitro_2009,
title = {In vitro behavior of multifunctionalized fullerene-warfarin conjugates},
author = {Marina Zacchigna and Cedric Klumpp and Maurizio Prato and Alberto Bianco},
doi = {10.1166/jnn.2009.1551},
issn = {1533-4880},
year = {2009},
date = {2009-10-01},
journal = {Journal of Nanoscience and Nanotechnology},
volume = {9},
number = {10},
pages = {6210--6221},
abstract = {In this study we have covalently linked the anticoagulant warfarin to polyfunctionalized fullerenes. The objective was to explore the possibility of modifying the biological profile of a drug by covalent binding to functionalized fullerene. We have chosen warfarin as a model compound because it a widely used drug. We have analyzed the stability in vitro of the conjugates and found that the drug is released from the carbon support only after incubation in mouse plasma.},
keywords = {Animals, Anticoagulants, Fullerenes, I2CT, In Vitro Techniques, Mice, Spectrophotometry, Team-Bianco, Ultraviolet, Warfarin},
pubstate = {published},
tppubtype = {article}
}
Klumpp Cédric, Lacerda Lara, Chaloin Olivier, Ros Tatiana Da, Kostarelos Kostas, Prato Maurizio, Bianco Alberto
Multifunctionalised cationic fullerene adducts for gene transfer: design, synthesis and DNA complexation Article de journal
Dans: Chemical Communications (Cambridge, England), no. 36, p. 3762–3764, 2007, ISSN: 1359-7345.
Résumé | Liens | BibTeX | Étiquettes: DNA, Electrophoresis, Fullerenes, Gene Transfer Techniques, I2CT, Molecular Structure, Plasmids, Team-Bianco
@article{klumpp_multifunctionalised_2007,
title = {Multifunctionalised cationic fullerene adducts for gene transfer: design, synthesis and DNA complexation},
author = {Cédric Klumpp and Lara Lacerda and Olivier Chaloin and Tatiana Da Ros and Kostas Kostarelos and Maurizio Prato and Alberto Bianco},
doi = {10.1039/b708435h},
issn = {1359-7345},
year = {2007},
date = {2007-01-01},
journal = {Chemical Communications (Cambridge, England)},
number = {36},
pages = {3762--3764},
abstract = {Cationic poly-N,N-dimethylfulleropyrrolidinium derivatives have been designed and synthesised to complex plasmid DNA for gene delivery.},
keywords = {DNA, Electrophoresis, Fullerenes, Gene Transfer Techniques, I2CT, Molecular Structure, Plasmids, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Pastorin Giorgia, Marchesan Silvia, Hoebeke Johan, Ros Tatiana Da, Ehret-Sabatier Laurence, Briand Jean-Paul, Prato Maurizio, Bianco Alberto
Design and activity of cationic fullerene derivatives as inhibitors of acetylcholinesterase Article de journal
Dans: Organic & Biomolecular Chemistry, vol. 4, no. 13, p. 2556–2562, 2006, ISSN: 1477-0520.
Résumé | Liens | BibTeX | Étiquettes: Acetylcholinesterase, Binding Sites, Cations, Cholinesterase Inhibitors, Drug Design, Fullerenes, I2CT, Models, Molecular, Team-Bianco
@article{pastorin_design_2006,
title = {Design and activity of cationic fullerene derivatives as inhibitors of acetylcholinesterase},
author = {Giorgia Pastorin and Silvia Marchesan and Johan Hoebeke and Tatiana Da Ros and Laurence Ehret-Sabatier and Jean-Paul Briand and Maurizio Prato and Alberto Bianco},
doi = {10.1039/b604361e},
issn = {1477-0520},
year = {2006},
date = {2006-07-01},
journal = {Organic & Biomolecular Chemistry},
volume = {4},
number = {13},
pages = {2556--2562},
abstract = {Four different regioisomers of cationic bis-N,N-dimethylfulleropyrrolidinium salts have been prepared and evaluated as inhibitors of the enzymatic activity of acetylcholinesterase. These fullerene-based derivatives were found to be noncompetitive inhibitors of acetylthiocholine hydrolysis. Molecular modelling was used to describe the possible interactions between the fullerene cage and the amino acids surrounding the cavity of the enzyme. The cationic C(60) derivatives used in this study represent a new class of molecules potentially able to modulate the enzymatic activity of acetylcholinesterase.},
keywords = {Acetylcholinesterase, Binding Sites, Cations, Cholinesterase Inhibitors, Drug Design, Fullerenes, I2CT, Models, Molecular, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Bianco Alberto, Maggini Michele, Nogarole Marco, Scorrano Gianfranco
Hydrolysis Rate of Functionalized Fullerenes Bearing Alkoxysilanes: A Comparative Study Article de journal
Dans: European Journal of Organic Chemistry, vol. 2006, no. 13, p. 2934–2941, 2006, ISSN: 1434-193X.
Résumé | Liens | BibTeX | Étiquettes: Alkoxysilanes, Fullerenes, Fulleropyrrolidines, I2CT, Sol–gel, Team-Bianco
@article{bianco_hydrolysis_2006,
title = {Hydrolysis Rate of Functionalized Fullerenes Bearing Alkoxysilanes: A Comparative Study},
author = {Alberto Bianco and Michele Maggini and Marco Nogarole and Gianfranco Scorrano},
url = {https://chemistry-europe.onlinelibrary.wiley.com/doi/abs/10.1002/ejoc.200600084},
doi = {10.1002/ejoc.200600084},
issn = {1434-193X},
year = {2006},
date = {2006-07-01},
urldate = {2020-03-31},
journal = {European Journal of Organic Chemistry},
volume = {2006},
number = {13},
pages = {2934--2941},
abstract = {Abstract Soluble fulleropyrrolidines bearing a trialkoxysilyl functionality (methoxy, ethoxy, butoxy, and isopropoxy) have been prepared and characterized. The hydrolysis rate constant for each fulleropyrrolidine was measured with 1H NMR spectroscopy by following the disappearance of selected resonances of the fullerene substrate under the conditions (HCl/H2O/THF) used for the preparation of fullerene-doped sol?gel glasses. It has been found that fulleropyrrolidine 1, bearing the trimethoxysilyl group, hydrolyzes faster than substrates 2?7 and should be the reagent of choice to minimize aggregation of the fullerene spheroid in sol?gel glassy matrices. The triethoxysilyl derivative 2, our benchmark fulleropyrrolidine for incorporation in sol?gel glasses, has the secondfastest hydrolysis rate. (? Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2006)},
keywords = {Alkoxysilanes, Fullerenes, Fulleropyrrolidines, I2CT, Sol–gel, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Brough Peter, Klumpp Cedric, Bianco Alberto, Campidelli Stephane, Prato Maurizio
[60]fullerene-pyrrolidine-N-oxides Article de journal
Dans: The Journal of Organic Chemistry, vol. 71, no. 5, p. 2014–2020, 2006, ISSN: 0022-3263.
Résumé | Liens | BibTeX | Étiquettes: Chromatography, Fullerenes, High Pressure Liquid, I2CT, Nitrogen, Oxidation-Reduction, Oxides, Pyrrolidines, Spectrum Analysis, Team-Bianco
@article{brough_60fullerene-pyrrolidine-n-oxides_2006,
title = {[60]fullerene-pyrrolidine-N-oxides},
author = {Peter Brough and Cedric Klumpp and Alberto Bianco and Stephane Campidelli and Maurizio Prato},
doi = {10.1021/jo052388s},
issn = {0022-3263},
year = {2006},
date = {2006-03-01},
journal = {The Journal of Organic Chemistry},
volume = {71},
number = {5},
pages = {2014--2020},
abstract = {Eight members of a new family of fullerene derivatives, [60]fulleropyrrolidine-N-oxides, have been synthesized and characterized. Facile oxidation, by a peracid, of the parent [60]fulleropyrrolidine gave clean conversions into the product molecules, in which the tertiary amine is transformed into a quaternary amine bearing an oxygen atom. The reaction is very selective, favoring the nitrogen atom of the pyrrolidine ring in preference to epoxidation of the fullerene cage. The 1H NMR shows an AB quartet splitting pattern, characteristic of nonequivalent hydrogens in the pyrrolidine ring and at a chemical shift displacement of 0.8 ppm downfield. Other methods of characterization are described, including MS, differential scanning calorimetry, thermogravimetric analysis, HPLC, UV/vis, and IR. Conclusive evidence for the formation of an N-oxide moiety is provided by the synthesis, oxidation, and NMR characterization of a novel [60]fulleropyrrolidine containing a 15N isotope, showing an 85 ppm downfield heteroatom chemical shift. Preliminary details of the effects of substitution on the reactivity of the pyrrolidine ring are also reported.},
keywords = {Chromatography, Fullerenes, High Pressure Liquid, I2CT, Nitrogen, Oxidation-Reduction, Oxides, Pyrrolidines, Spectrum Analysis, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Bianco Alberto
Efficient solid-phase synthesis of fullero-peptides using Merrifield strategy Article de journal
Dans: Chemical Communications (Cambridge, England), no. 25, p. 3174–3176, 2005, ISSN: 1359-7345.
Résumé | Liens | BibTeX | Étiquettes: Chromatography, Fullerenes, High Pressure Liquid, I2CT, Mass Spectrometry, Peptides, Team-Bianco
@article{bianco_efficient_2005,
title = {Efficient solid-phase synthesis of fullero-peptides using Merrifield strategy},
author = {Alberto Bianco},
doi = {10.1039/b504659a},
issn = {1359-7345},
year = {2005},
date = {2005-07-01},
journal = {Chemical Communications (Cambridge, England)},
number = {25},
pages = {3174--3176},
abstract = {Boc-protected l-fulleropyrrolidino-glutamic acid was readily prepared and employed for the synthesis of fullerene-containing peptides using the solid-phase Boc chemistry developed by Merrifield.},
keywords = {Chromatography, Fullerenes, High Pressure Liquid, I2CT, Mass Spectrometry, Peptides, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Pantarotto Davide, Tagmatarchis Nikos, Bianco Alberto, Prato Maurizio
Synthesis and biological properties of fullerene-containing amino acids and peptides Article de journal
Dans: Mini Reviews in Medicinal Chemistry, vol. 4, no. 7, p. 805–814, 2004, ISSN: 1389-5575.
Résumé | BibTeX | Étiquettes: Amino Acids, Animals, Fullerenes, Humans, I2CT, Molecular Structure, Peptides, Solubility, Team-Bianco
@article{pantarotto_synthesis_2004,
title = {Synthesis and biological properties of fullerene-containing amino acids and peptides},
author = {Davide Pantarotto and Nikos Tagmatarchis and Alberto Bianco and Maurizio Prato},
issn = {1389-5575},
year = {2004},
date = {2004-09-01},
journal = {Mini Reviews in Medicinal Chemistry},
volume = {4},
number = {7},
pages = {805--814},
abstract = {Organofullerene derivatives have shown a great potential in a wide variety of biological activities such as DNA photocleavage, HIV-protease inhibition, neuroprotection and apoptosis. Among the plethora of functionalized organofullerenes that have been synthesized, fullerene-based amino acids are particularly appealing for structural studies and biological applications. When the fullerene-framework is incorporated into peptides, its original properties can be substantially modified. In addition, the water-solubility of the fullerene derivatives is enhanced, which makes such molecules amenable to biological studies. In this review, recent advances in the growing field of medicinal chemistry of fullerene derivatives will be discussed. Emphasis will be given to the synthesis of the biggest unnatural amino acid 3,4-fulleroproline (Fpr) and its derivatives. For example, Fpr derivatives have been found to interact with different hydrolytic enzymes and selectively discriminate between rationally designed peptides. Fullerene-based peptides have been found to substantially activate enzymes involved in the oxidative deamination of biogenic amines. In addition, their membranotropic properties and effects on the structure and permeability of the lipid bilayer of phosphatidylcholine liposomes as well as the transmembrane transport of bivalent metal ions have been studied. Finally, applications in medicinal chemistry of such types of amino acids and peptides will be highlighted.},
keywords = {Amino Acids, Animals, Fullerenes, Humans, I2CT, Molecular Structure, Peptides, Solubility, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Bianco Alberto, Pantarotto Davide, Hoebeke Johan, Briand Jean-Paul, Prato Maurizio
Solid-phase synthesis and characterization of a novel fullerene-peptide derived from histone H3 Article de journal
Dans: Organic & Biomolecular Chemistry, vol. 1, no. 23, p. 4141–4143, 2003, ISSN: 1477-0520.
Résumé | Liens | BibTeX | Étiquettes: Chromatography, Epitopes, Fullerenes, Glutamic Acid, High Pressure Liquid, Histones, I2CT, Models, Molecular, Molecular Structure, Peptides, Protein Structure, Team-Bianco, Tertiary
@article{bianco_solid-phase_2003,
title = {Solid-phase synthesis and characterization of a novel fullerene-peptide derived from histone H3},
author = {Alberto Bianco and Davide Pantarotto and Johan Hoebeke and Jean-Paul Briand and Maurizio Prato},
doi = {10.1039/b311505d},
issn = {1477-0520},
year = {2003},
date = {2003-12-01},
journal = {Organic & Biomolecular Chemistry},
volume = {1},
number = {23},
pages = {4141--4143},
abstract = {A peptide analogue from a histone H3 protein containing the L-fulleropyrrolidino-glutamic acid has been prepared by a solid-phase approach and has been fully characterized. By molecular modelling it was verified that this peptide derivative is able to retain a binding capacity to the MHC (major histocompatibility complex) molecule similar to that of the cognate epitope.},
keywords = {Chromatography, Epitopes, Fullerenes, Glutamic Acid, High Pressure Liquid, Histones, I2CT, Models, Molecular, Molecular Structure, Peptides, Protein Structure, Team-Bianco, Tertiary},
pubstate = {published},
tppubtype = {article}
}
Pantarotto Davide, Bianco Alberto, Pellarini Federica, Tossi Alessandro, Giangaspero Anna, Zelezetsky Igor, Briand Jean-Paul, Prato Maurizio
Solid-phase synthesis of fullerene-peptides Article de journal
Dans: Journal of the American Chemical Society, vol. 124, no. 42, p. 12543–12549, 2002, ISSN: 0002-7863.
Résumé | Liens | BibTeX | Étiquettes: Amino Acids, Anti-Bacterial Agents, Anti-Infective Agents, Candida albicans, Electrospray Ionization, Enkephalin, Escherichia coli, Fluorenes, Fullerenes, I2CT, Leucine, Mass, Microbial Sensitivity Tests, Oligopeptides, Spectrometry, Staphylococcus aureus, Team-Bianco
@article{pantarotto_solid-phase_2002,
title = {Solid-phase synthesis of fullerene-peptides},
author = {Davide Pantarotto and Alberto Bianco and Federica Pellarini and Alessandro Tossi and Anna Giangaspero and Igor Zelezetsky and Jean-Paul Briand and Maurizio Prato},
doi = {10.1021/ja027603q},
issn = {0002-7863},
year = {2002},
date = {2002-10-01},
journal = {Journal of the American Chemical Society},
volume = {124},
number = {42},
pages = {12543--12549},
abstract = {The solid-phase synthesis of peptides (SPPS) containing [60]fullerene-functionalized amino acids is reported. A new amino acid, fulleropyrrolidino-glutamic acid (Fgu), is used for the SPPS of a series of analogues of different length based on the natural Leu(5)-Enkephalin and on cationic antimicrobial peptides. These fullero-peptides were prepared on different solid supports to analyze the influence of the resin on the synthesis. Optimized protocols for the coupling and deprotection procedures were determined allowing the synthesis of highly pure peptides in sufficient quantities for evaluation of biological activities. In particular, to avoid side reactions of the fullerene moiety with bases and nucleophiles, the removal of the protecting groups was performed under inert conditions (nitrogen or argon in the dark). We have encountered serious problems with the recovery of the crude compounds, especially when Fgu was inserted in the proximity of the resin core as fullero-peptides tend to remain embedded inside the resin. Eventually, all of the fullero-peptides were easily purified, and the cationic peptides were tested for their antimicrobial activities. They displayed a specific activity against the Gram-positive bacterium S. aureus and also lysed erythrocytes. The availability of a fullero-amino acid easily useable in the SPPS of fullero-peptides may thus open the way to the synthesis of new types of biologically active oligomers.},
keywords = {Amino Acids, Anti-Bacterial Agents, Anti-Infective Agents, Candida albicans, Electrospray Ionization, Enkephalin, Escherichia coli, Fluorenes, Fullerenes, I2CT, Leucine, Mass, Microbial Sensitivity Tests, Oligopeptides, Spectrometry, Staphylococcus aureus, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Bianco A, Ros T Da, Prato M, Toniolo C
Fullerene-based amino acids and peptides Article de journal
Dans: Journal of Peptide Science: An Official Publication of the European Peptide Society, vol. 7, no. 4, p. 208–219, 2001, ISSN: 1075-2617.
Résumé | Liens | BibTeX | Étiquettes: Amino Acids, Animals, Antiviral Agents, carbon, Fullerenes, Humans, I2CT, Infections, Oxidative Stress, Peptides, Proline, Team-Bianco
@article{bianco_fullerene-based_2001,
title = {Fullerene-based amino acids and peptides},
author = {A Bianco and T Da Ros and M Prato and C Toniolo},
doi = {10.1002/psc.313},
issn = {1075-2617},
year = {2001},
date = {2001-04-01},
journal = {Journal of Peptide Science: An Official Publication of the European Peptide Society},
volume = {7},
number = {4},
pages = {208--219},
abstract = {Recent advances in the chemistry of fullerene have allowed the synthesis of many classes of novel fullerene derivatives. Among these classes, fullerene-based amino acids and peptides are particularly interesting, both for structural studies and biological applications. In this review, we will discuss our own achievements in this rapidly growing field. In particular, the application of fulleroproline (Fpr) amino acids and peptides to medicinal chemistry and material science will be highlighted.},
keywords = {Amino Acids, Animals, Antiviral Agents, carbon, Fullerenes, Humans, I2CT, Infections, Oxidative Stress, Peptides, Proline, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}