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2005
Kostarelos K, Lacerda L, Partidos C D, Prato M, Bianco A
Carbon nanotube-mediated delivery of peptides and genes to cells: translating nanobiotechnology to therapeutics Article de journal
Dans: Journal of Drug Delivery Science and Technology, vol. 15, no. 1, p. 41–47, 2005, ISSN: 1773-2247.
Résumé | Liens | BibTeX | Étiquettes: Carbon nanotubes, gene delivery, gene therapy, I2CT, Nanomedicine, Peptide delivery, Team-Bianco, Vaccination
@article{kostarelos_carbon_2005,
title = {Carbon nanotube-mediated delivery of peptides and genes to cells: translating nanobiotechnology to therapeutics},
author = {K Kostarelos and L Lacerda and C D Partidos and M Prato and A Bianco},
url = {http://www.sciencedirect.com/science/article/pii/S1773224705500054},
doi = {10.1016/S1773-2247(05)50005-4},
issn = {1773-2247},
year = {2005},
date = {2005-01-01},
urldate = {2020-03-31},
journal = {Journal of Drug Delivery Science and Technology},
volume = {15},
number = {1},
pages = {41--47},
abstract = {During the last few years, there has been a tremendous amount of optimism and expectation about nanotechnology and its impact on various fields including medicine and pharmaceutical development. One of the most promising materials being developed during the nanotechnological renaissance we are currently experiencing is the carbon nanotube. Before any biology-related application can even be envisaged, the aqueous solubility of carbon nanotubes has to be resolved. Recently, a variety of methodologies have been proposed which lead to biologically compatible carbon nanotubes. Covalent functionalization of their surface is one methodology, allowing the first attempts towards applications in the field of nanomedicine. The possibility of incorporating functionalized carbon nanotubes into cells and the biological milieu offers numerous advantages for potential applications in biology and pharmacology. One of the most promising is their utilization as a new carrier system for the delivery of therapeutic molecules. In the present article, the first attempts to transform carbon nanotubes from biologically incompatible nanomaterials to biologically relevant components of advanced therapeutics and the ensuing novel structures obtained in our laboratories are presented.},
keywords = {Carbon nanotubes, gene delivery, gene therapy, I2CT, Nanomedicine, Peptide delivery, Team-Bianco, Vaccination},
pubstate = {published},
tppubtype = {article}
}
During the last few years, there has been a tremendous amount of optimism and expectation about nanotechnology and its impact on various fields including medicine and pharmaceutical development. One of the most promising materials being developed during the nanotechnological renaissance we are currently experiencing is the carbon nanotube. Before any biology-related application can even be envisaged, the aqueous solubility of carbon nanotubes has to be resolved. Recently, a variety of methodologies have been proposed which lead to biologically compatible carbon nanotubes. Covalent functionalization of their surface is one methodology, allowing the first attempts towards applications in the field of nanomedicine. The possibility of incorporating functionalized carbon nanotubes into cells and the biological milieu offers numerous advantages for potential applications in biology and pharmacology. One of the most promising is their utilization as a new carrier system for the delivery of therapeutic molecules. In the present article, the first attempts to transform carbon nanotubes from biologically incompatible nanomaterials to biologically relevant components of advanced therapeutics and the ensuing novel structures obtained in our laboratories are presented.
Fournel Sylvie, Wieckowski Sébastien, Sun Weimin, Trouche Nathalie, Dumortier Hélène, Bianco Alberto, Chaloin Olivier, Habib Mohammed, Peter Jean-Christophe, Schneider Pascal, Vray Bernard, Toes René E, Offringa Rienk, Melief Cornelis J M, Hoebeke Johan, Guichard Gilles
C3-symmetric peptide scaffolds are functional mimetics of trimeric CD40L Article de journal
Dans: Nature Chemical Biology, vol. 1, no. 7, p. 377–382, 2005, ISSN: 1552-4450.
Résumé | Liens | BibTeX | Étiquettes: Animals, Apoptosis, Biological, CD40 Antigens, CD40 Ligand, Cell Line, Humans, I2CT, Inbred BALB C, Mice, Models, Molecular Mimicry, Molecular Structure, Peptides, Protein Conformation, Protein Structure, Quaternary, Structure-Activity Relationship, Team-Bianco, Time Factors, tumor
@article{fournel_c3-symmetric_2005b,
title = {C3-symmetric peptide scaffolds are functional mimetics of trimeric CD40L},
author = {Sylvie Fournel and Sébastien Wieckowski and Weimin Sun and Nathalie Trouche and Hélène Dumortier and Alberto Bianco and Olivier Chaloin and Mohammed Habib and Jean-Christophe Peter and Pascal Schneider and Bernard Vray and René E Toes and Rienk Offringa and Cornelis J M Melief and Johan Hoebeke and Gilles Guichard},
doi = {10.1038/nchembio746},
issn = {1552-4450},
year = {2005},
date = {2005-01-01},
journal = {Nature Chemical Biology},
volume = {1},
number = {7},
pages = {377--382},
abstract = {Interaction between CD40, a member of the tumor necrosis factor receptor (TNFR) superfamily, and its ligand CD40L, a 39-kDa glycoprotein, is essential for the development of humoral and cellular immune responses. Selective blockade or activation of this pathway provides the ground for the development of new treatments against immunologically based diseases and malignancies. Like other members of the TNF superfamily, CD40L monomers self-assemble around a threefold symmetry axis to form noncovalent homotrimers that can each bind three receptor molecules. Here, we report on the structure-based design of small synthetic molecules with C3 symmetry that can mimic CD40L homotrimers. These molecules interact with CD40, compete with the binding of CD40L to CD40, and reproduce, to a certain extent, the functional properties of the much larger homotrimeric soluble CD40L. Architectures based on rigid C3-symmetric cores may thus represent a general approach to mimicking homotrimers of the TNF superfamily.},
keywords = {Animals, Apoptosis, Biological, CD40 Antigens, CD40 Ligand, Cell Line, Humans, I2CT, Inbred BALB C, Mice, Models, Molecular Mimicry, Molecular Structure, Peptides, Protein Conformation, Protein Structure, Quaternary, Structure-Activity Relationship, Team-Bianco, Time Factors, tumor},
pubstate = {published},
tppubtype = {article}
}
Interaction between CD40, a member of the tumor necrosis factor receptor (TNFR) superfamily, and its ligand CD40L, a 39-kDa glycoprotein, is essential for the development of humoral and cellular immune responses. Selective blockade or activation of this pathway provides the ground for the development of new treatments against immunologically based diseases and malignancies. Like other members of the TNF superfamily, CD40L monomers self-assemble around a threefold symmetry axis to form noncovalent homotrimers that can each bind three receptor molecules. Here, we report on the structure-based design of small synthetic molecules with C3 symmetry that can mimic CD40L homotrimers. These molecules interact with CD40, compete with the binding of CD40L to CD40, and reproduce, to a certain extent, the functional properties of the much larger homotrimeric soluble CD40L. Architectures based on rigid C3-symmetric cores may thus represent a general approach to mimicking homotrimers of the TNF superfamily.
Bianco Alberto, Kostarelos Kostas, Partidos Charalambos D, Prato Maurizio
Biomedical applications of functionalised carbon nanotubes Article de journal
Dans: Chemical Communications (Cambridge, England), no. 5, p. 571–577, 2005, ISSN: 1359-7345.
Résumé | Liens | BibTeX | Étiquettes: Antigens, carbon, Chemical, Drug Delivery Systems, Gene Transfer Techniques, Humans, I2CT, Models, Molecular Structure, nanotechnology, Nanotubes, Team-Bianco, Vaccines
@article{bianco_biomedical_2005,
title = {Biomedical applications of functionalised carbon nanotubes},
author = {Alberto Bianco and Kostas Kostarelos and Charalambos D Partidos and Maurizio Prato},
doi = {10.1039/b410943k},
issn = {1359-7345},
year = {2005},
date = {2005-01-01},
journal = {Chemical Communications (Cambridge, England)},
number = {5},
pages = {571--577},
abstract = {The organic functionalisation of carbon nanotubes can improve substantially their solubility and biocompatibility profile; as a consequence, their manipulation and integration into biological systems has become possible so that functionalised carbon nanotubes hold currently strong promise as novel systems for the delivery of drugs, antigens and genes.},
keywords = {Antigens, carbon, Chemical, Drug Delivery Systems, Gene Transfer Techniques, Humans, I2CT, Models, Molecular Structure, nanotechnology, Nanotubes, Team-Bianco, Vaccines},
pubstate = {published},
tppubtype = {article}
}
The organic functionalisation of carbon nanotubes can improve substantially their solubility and biocompatibility profile; as a consequence, their manipulation and integration into biological systems has become possible so that functionalised carbon nanotubes hold currently strong promise as novel systems for the delivery of drugs, antigens and genes.
Bianco Alberto, Hoebeke Johan, Godefroy Sylvie, Chaloin Olivier, Pantarotto Davide, Briand Jean-Paul, Muller Sylviane, Prato Maurizio, Partidos Charalambos D
Cationic carbon nanotubes bind to CpG oligodeoxynucleotides and enhance their immunostimulatory properties Article de journal
Dans: Journal of the American Chemical Society, vol. 127, no. 1, p. 58–59, 2005, ISSN: 0002-7863.
Résumé | Liens | BibTeX | Étiquettes: Adjuvants, Animals, carbon, Cations, CpG Islands, I2CT, Immunologic, Interferon-gamma, Interleukin-6, Kinetics, Lymphocytes, Mice, Nanotubes, oligonucleotides, Surface Plasmon Resonance, Team-Bianco
@article{bianco_cationic_2005,
title = {Cationic carbon nanotubes bind to CpG oligodeoxynucleotides and enhance their immunostimulatory properties},
author = {Alberto Bianco and Johan Hoebeke and Sylvie Godefroy and Olivier Chaloin and Davide Pantarotto and Jean-Paul Briand and Sylviane Muller and Maurizio Prato and Charalambos D Partidos},
doi = {10.1021/ja044293y},
issn = {0002-7863},
year = {2005},
date = {2005-01-01},
journal = {Journal of the American Chemical Society},
volume = {127},
number = {1},
pages = {58--59},
abstract = {Functionalized cationic carbon nanotubes are able to form a stable complex with CpG ODN based on charge interaction and to increase the immunostimulatory activity of CpG motifs.},
keywords = {Adjuvants, Animals, carbon, Cations, CpG Islands, I2CT, Immunologic, Interferon-gamma, Interleukin-6, Kinetics, Lymphocytes, Mice, Nanotubes, oligonucleotides, Surface Plasmon Resonance, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Functionalized cationic carbon nanotubes are able to form a stable complex with CpG ODN based on charge interaction and to increase the immunostimulatory activity of CpG motifs.
2004
Bianco Alberto
Carbon nanotubes for the delivery of therapeutic molecules Article de journal
Dans: Expert Opinion on Drug Delivery, vol. 1, no. 1, p. 57–65, 2004, ISSN: 1742-5247.
Résumé | Liens | BibTeX | Étiquettes: carbon, Drug Carriers, Gene Transfer Techniques, I2CT, Nanotubes, Pharmaceutical Preparations, Team-Bianco
@article{bianco_carbon_2004,
title = {Carbon nanotubes for the delivery of therapeutic molecules},
author = {Alberto Bianco},
doi = {10.1517/17425247.1.1.57},
issn = {1742-5247},
year = {2004},
date = {2004-11-01},
journal = {Expert Opinion on Drug Delivery},
volume = {1},
number = {1},
pages = {57--65},
abstract = {Functionalised carbon nanotubes (f-CNTs) are emerging as new tools in the field of nanobiotechnology and nanomedicine. This is because they can be easily manipulated and modified by encapsulation with biopolymers or by covalent linking of solubilising groups to the external walls and tips. The possibility of incorporating f-CNTs into biological systems has opened the way to the exploration of their potential applications in biology and medicinal chemistry. Within the different fields of applications (i.e., biosensors, composite materials, molecular electronics), one use of CNTs is as new carrier systems for the delivery of therapeutic molecules. Research discussed in this review is focused on recent advances in the development of CNT technology for the delivery of drugs, antigens and genes.},
keywords = {carbon, Drug Carriers, Gene Transfer Techniques, I2CT, Nanotubes, Pharmaceutical Preparations, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Functionalised carbon nanotubes (f-CNTs) are emerging as new tools in the field of nanobiotechnology and nanomedicine. This is because they can be easily manipulated and modified by encapsulation with biopolymers or by covalent linking of solubilising groups to the external walls and tips. The possibility of incorporating f-CNTs into biological systems has opened the way to the exploration of their potential applications in biology and medicinal chemistry. Within the different fields of applications (i.e., biosensors, composite materials, molecular electronics), one use of CNTs is as new carrier systems for the delivery of therapeutic molecules. Research discussed in this review is focused on recent advances in the development of CNT technology for the delivery of drugs, antigens and genes.
Poschalko Alexander, Lancelot Nathalie, Marin Julien, Larras Virginie, Limal David, Elbayed Karim, Raya Jesus, Piotto Martial, Briand Jean-Paul, Guichard Gilles, Bianco Alberto
DEUSS: A Perdeuterated Poly(oxyethylene)-Based Resin for Improving HRMAS NMR Studies of Solid-Supported Molecules Article de journal
Dans: Chemistry – A European Journal, vol. 10, no. 18, p. 4532–4537, 2004, ISSN: 0947-6539.
Résumé | Liens | BibTeX | Étiquettes: combinatorial chemistry, I2CT, NMR spectroscopy, oligoureas, Peptides, poly(oxyethylene), Resins, Team-Bianco
@article{poschalko_deuss_2004,
title = {DEUSS: A Perdeuterated Poly(oxyethylene)-Based Resin for Improving HRMAS NMR Studies of Solid-Supported Molecules},
author = {Alexander Poschalko and Nathalie Lancelot and Julien Marin and Virginie Larras and David Limal and Karim Elbayed and Jesus Raya and Martial Piotto and Jean-Paul Briand and Gilles Guichard and Alberto Bianco},
url = {https://chemistry-europe.onlinelibrary.wiley.com/doi/abs/10.1002/chem.200400373},
doi = {10.1002/chem.200400373},
issn = {0947-6539},
year = {2004},
date = {2004-09-01},
urldate = {2020-03-31},
journal = {Chemistry – A European Journal},
volume = {10},
number = {18},
pages = {4532--4537},
abstract = {Abstract A novel resin called DEUSS (perdeuterated poly(oxyethylene)-based solid support) has been prepared by anionic polymerization of deuterated [D4]ethylene oxide, followed by cross-linking with deuterated epichlorohydrin. DEUSS can be suspended in a wide range of solvents including organic and aqueous solutions, in which it displays a high swelling capacity. As measured by proton HRMAS of the swollen polymer, the signal intensity of the oxyethylene protons is reduced by a factor of 110 relative to the corresponding nondeuterated poly(oxyethylene)poly(oxypropylene) (POEPOP) resin, thus facilitating detailed HRMAS NMR studies of covalently linked molecules. This 1H NMR invisible matrix was used for the solid-phase synthesis of peptides, oligoureas, and a series of amides as well as their characterization by HRMAS NMR spectroscopy. On-bead NMR spectra of high quality and with resolution comparable to that of liquid samples were obtained and readily interpreted. The complete absence of the parasite resin signals will be of great advantage, for example, for the optimization of multistep solid-phase stereoselective reactions, and for the conformational study of resin-bound molecules in a large variety of solvents.},
keywords = {combinatorial chemistry, I2CT, NMR spectroscopy, oligoureas, Peptides, poly(oxyethylene), Resins, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Abstract A novel resin called DEUSS (perdeuterated poly(oxyethylene)-based solid support) has been prepared by anionic polymerization of deuterated [D4]ethylene oxide, followed by cross-linking with deuterated epichlorohydrin. DEUSS can be suspended in a wide range of solvents including organic and aqueous solutions, in which it displays a high swelling capacity. As measured by proton HRMAS of the swollen polymer, the signal intensity of the oxyethylene protons is reduced by a factor of 110 relative to the corresponding nondeuterated poly(oxyethylene)poly(oxypropylene) (POEPOP) resin, thus facilitating detailed HRMAS NMR studies of covalently linked molecules. This 1H NMR invisible matrix was used for the solid-phase synthesis of peptides, oligoureas, and a series of amides as well as their characterization by HRMAS NMR spectroscopy. On-bead NMR spectra of high quality and with resolution comparable to that of liquid samples were obtained and readily interpreted. The complete absence of the parasite resin signals will be of great advantage, for example, for the optimization of multistep solid-phase stereoselective reactions, and for the conformational study of resin-bound molecules in a large variety of solvents.
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}
}
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.
Lancelot Nathalie, Elbayed Karim, Bianco Alberto, Piotto Martial
Measurement of scaled residual dipolar couplings in proteins using variable-angle sample spinning Article de journal
Dans: Journal of biomolecular NMR, vol. 29, no. 3, p. 259–269, 2004, ISSN: 0925-2738.
Résumé | Liens | BibTeX | Étiquettes: anisotropy, I2CT, Magnetic Resonance Spectroscopy, Magnetics, Models, Phospholipid Ethers, Proteins, Statistical, Team-Bianco, Temperature, ubiquitin
@article{lancelot_measurement_2004,
title = {Measurement of scaled residual dipolar couplings in proteins using variable-angle sample spinning},
author = {Nathalie Lancelot and Karim Elbayed and Alberto Bianco and Martial Piotto},
doi = {10.1023/B:JNMR.0000032548.60663.1f},
issn = {0925-2738},
year = {2004},
date = {2004-07-01},
journal = {Journal of biomolecular NMR},
volume = {29},
number = {3},
pages = {259--269},
abstract = {NMR spectra of ubiquitin in the presence of bicelles at a concentration of 25% w/v have been recorded under sample spinning conditions for different angles of rotation. For an axis of rotation equal to the magic angle, the (1)H/(15)N HSQC recorded without any (1)H decoupling in the indirect dimension corresponds to the classical spectrum obtained on a protein in an isotropic solution and allows the measurement of scalar J-couplings (1) J (NH). For an angle of rotation smaller than the magic angle, the bicelles orient with their normal perpendicular to the spinning axis, whereas for an angle of rotation greater than the magic angle the bicelles orient with their normal along the spinning axis. This bicelle alignment creates anisotropic conditions that give rise to the observation of residual dipolar couplings in ubiquitin. The magnitude of these dipolar couplings depends directly on the angle that the rotor makes with the main magnetic field. By changing this angle in a controlled manner, residual dipolar couplings can be either scaled up or down thus offering the possibility to study simultaneously a wide range of dipolar couplings in the same sample.},
keywords = {anisotropy, I2CT, Magnetic Resonance Spectroscopy, Magnetics, Models, Phospholipid Ethers, Proteins, Statistical, Team-Bianco, Temperature, ubiquitin},
pubstate = {published},
tppubtype = {article}
}
NMR spectra of ubiquitin in the presence of bicelles at a concentration of 25% w/v have been recorded under sample spinning conditions for different angles of rotation. For an axis of rotation equal to the magic angle, the (1)H/(15)N HSQC recorded without any (1)H decoupling in the indirect dimension corresponds to the classical spectrum obtained on a protein in an isotropic solution and allows the measurement of scalar J-couplings (1) J (NH). For an angle of rotation smaller than the magic angle, the bicelles orient with their normal perpendicular to the spinning axis, whereas for an angle of rotation greater than the magic angle the bicelles orient with their normal along the spinning axis. This bicelle alignment creates anisotropic conditions that give rise to the observation of residual dipolar couplings in ubiquitin. The magnitude of these dipolar couplings depends directly on the angle that the rotor makes with the main magnetic field. By changing this angle in a controlled manner, residual dipolar couplings can be either scaled up or down thus offering the possibility to study simultaneously a wide range of dipolar couplings in the same sample.
Pantarotto Davide, Singh Ravi, McCarthy David, Erhardt Mathieu, Briand Jean-Paul, Prato Maurizio, Kostarelos Kostas, Bianco Alberto
Functionalized Carbon Nanotubes for Plasmid DNA Gene Delivery Article de journal
Dans: Angewandte Chemie International Edition, vol. 43, no. 39, p. 5242–5246, 2004, ISSN: 1521-3773.
Résumé | Liens | BibTeX | Étiquettes: Carbon nanotubes, gene delivery, I2CT, plasmid DNA, supramolecular chemistry, Team-Bianco
@article{pantarotto_functionalized_2004,
title = {Functionalized Carbon Nanotubes for Plasmid DNA Gene Delivery},
author = {Davide Pantarotto and Ravi Singh and David McCarthy and Mathieu Erhardt and Jean-Paul Briand and Maurizio Prato and Kostas Kostarelos and Alberto Bianco},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.200460437},
doi = {10.1002/anie.200460437},
issn = {1521-3773},
year = {2004},
date = {2004-01-01},
urldate = {2020-03-31},
journal = {Angewandte Chemie International Edition},
volume = {43},
number = {39},
pages = {5242--5246},
abstract = {Genetic vaccination and gene therapy research could benefit from the application of carbon nanotubes. Functionalized, positively charged, water-soluble carbon nanotubes are able to penetrate into cells (see figure) and can transport plasmid DNA by formation of noncovalent DNA–nanotube complexes. Such nanotubes can be used as novel nonviral delivery systems for gene transfer.},
keywords = {Carbon nanotubes, gene delivery, I2CT, plasmid DNA, supramolecular chemistry, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Genetic vaccination and gene therapy research could benefit from the application of carbon nanotubes. Functionalized, positively charged, water-soluble carbon nanotubes are able to penetrate into cells (see figure) and can transport plasmid DNA by formation of noncovalent DNA–nanotube complexes. Such nanotubes can be used as novel nonviral delivery systems for gene transfer.
Pantarotto Davide, Briand Jean-Paul, Prato Maurizio, Bianco Alberto
Translocation of bioactive peptides across cell membranes by carbon nanotubes Article de journal
Dans: Chemical Communications (Cambridge, England), no. 1, p. 16–17, 2004, ISSN: 1359-7345.
Résumé | Liens | BibTeX | Étiquettes: 3T3 Cells, Animals, carbon, Cell Membrane, Confocal, Flow Cytometry, fluorescence, I2CT, Mice, Microscopy, Nanotubes, Particle Size, Peptides, Protein Transport, Team-Bianco
@article{pantarotto_translocation_2004,
title = {Translocation of bioactive peptides across cell membranes by carbon nanotubes},
author = {Davide Pantarotto and Jean-Paul Briand and Maurizio Prato and Alberto Bianco},
doi = {10.1039/b311254c},
issn = {1359-7345},
year = {2004},
date = {2004-01-01},
journal = {Chemical Communications (Cambridge, England)},
number = {1},
pages = {16--17},
abstract = {Functionalised carbon nanotubes are able to cross the cell membrane and to accumulate in the cytoplasm or reach the nucleus without being toxic for the cell up to 10 [micro sign]M.},
keywords = {3T3 Cells, Animals, carbon, Cell Membrane, Confocal, Flow Cytometry, fluorescence, I2CT, Mice, Microscopy, Nanotubes, Particle Size, Peptides, Protein Transport, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Functionalised carbon nanotubes are able to cross the cell membrane and to accumulate in the cytoplasm or reach the nucleus without being toxic for the cell up to 10 [micro sign]M.
2003
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}
}
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.
Poschalko Alexander, Rohr Thomas, Gruber Heinrich, Bianco Alberto, Guichard Gilles, Briand Jean-Paul, Weber Viktoria, Falkenhagen Dieter
SUBPOL: A Novel Sucrose-Based Polymer Support for Solid-Phase Peptide Synthesis and Affinity Chromatography Applications Article de journal
Dans: Journal of the American Chemical Society, vol. 125, no. 44, p. 13415–13426, 2003, ISSN: 0002-7863, 1520-5126.
Liens | BibTeX | Étiquettes: I2CT, Team-Bianco
@article{poschalko_subpol_2003,
title = {SUBPOL: A Novel Sucrose-Based Polymer Support for Solid-Phase Peptide Synthesis and Affinity Chromatography Applications},
author = {Alexander Poschalko and Thomas Rohr and Heinrich Gruber and Alberto Bianco and Gilles Guichard and Jean-Paul Briand and Viktoria Weber and Dieter Falkenhagen},
url = {https://pubs.acs.org/doi/10.1021/ja035874a},
doi = {10.1021/ja035874a},
issn = {0002-7863, 1520-5126},
year = {2003},
date = {2003-11-01},
urldate = {2020-11-26},
journal = {Journal of the American Chemical Society},
volume = {125},
number = {44},
pages = {13415--13426},
keywords = {I2CT, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Pantarotto Davide, Partidos Charalambos D, Hoebeke Johan, Brown Fred, Kramer Ed, Briand Jean-Paul, Muller Sylviane, Prato Maurizio, Bianco Alberto
Immunization with Peptide-Functionalized Carbon Nanotubes Enhances Virus-Specific Neutralizing Antibody Responses Article de journal
Dans: Chemistry & Biology, vol. 10, no. 10, p. 961–966, 2003, ISSN: 1074-5521.
Résumé | Liens | BibTeX | Étiquettes: I2CT, Team-Bianco
@article{pantarotto_immunization_2003-1,
title = {Immunization with Peptide-Functionalized Carbon Nanotubes Enhances Virus-Specific Neutralizing Antibody Responses},
author = {Davide Pantarotto and Charalambos D Partidos and Johan Hoebeke and Fred Brown and Ed Kramer and Jean-Paul Briand and Sylviane Muller and Maurizio Prato and Alberto Bianco},
url = {http://www.sciencedirect.com/science/article/pii/S107455210300214X},
doi = {10.1016/j.chembiol.2003.09.011},
issn = {1074-5521},
year = {2003},
date = {2003-10-01},
urldate = {2020-03-31},
journal = {Chemistry & Biology},
volume = {10},
number = {10},
pages = {961--966},
abstract = {Functionalized carbon nanotubes (CNTs) hold a lot of promise for application in medicinal chemistry. Based on a method for preparation of water-soluble CNTs, we covalently linked a neutralizing B cell epitope from the foot-and-mouth disease virus (FMDV) to mono- and bis-derivatized CNTs. Immunological characterization of these conjugates revealed that the epitope was appropriately presented after conjugation to CNTs for recognition by antibodies as measured by BIAcore technology. Moreover, peptide-carbon nanotubes elicited strong anti-peptide antibody responses in mice with no detectable cross-reactivity to the carbon nanotubes. However, only the mono-derivitized CNT conjugate induced high levels of virus-neutralizing antibodies. These findings highlight for the first time the potential of CNTs to present biologically important epitopes in an appropriate conformation both in vitro and in vivo and open up the possibility for their use in vaccine delivery.},
keywords = {I2CT, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Functionalized carbon nanotubes (CNTs) hold a lot of promise for application in medicinal chemistry. Based on a method for preparation of water-soluble CNTs, we covalently linked a neutralizing B cell epitope from the foot-and-mouth disease virus (FMDV) to mono- and bis-derivatized CNTs. Immunological characterization of these conjugates revealed that the epitope was appropriately presented after conjugation to CNTs for recognition by antibodies as measured by BIAcore technology. Moreover, peptide-carbon nanotubes elicited strong anti-peptide antibody responses in mice with no detectable cross-reactivity to the carbon nanotubes. However, only the mono-derivitized CNT conjugate induced high levels of virus-neutralizing antibodies. These findings highlight for the first time the potential of CNTs to present biologically important epitopes in an appropriate conformation both in vitro and in vivo and open up the possibility for their use in vaccine delivery.
Pantarotto Davide, Partidos Charalambos D, Hoebeke Johan, Brown Fred, Kramer Ed, Briand Jean-Paul, Muller Sylviane, Prato Maurizio, Bianco Alberto
Immunization with peptide-functionalized carbon nanotubes enhances virus-specific neutralizing antibody responses Article de journal
Dans: Chemistry & Biology, vol. 10, no. 10, p. 961–966, 2003, ISSN: 1074-5521.
Liens | BibTeX | Étiquettes: Animals, Antibodies, Antigen-Antibody Reactions, carbon, Drug Delivery Systems, Epitopes, Foot-and-Mouth Disease Virus, I2CT, Immunization, Mice, Monoclonal, Nanotubes, Neutralization Tests, Peptides, Team-Bianco, Vaccines, Viral
@article{pantarotto_immunization_2003,
title = {Immunization with peptide-functionalized carbon nanotubes enhances virus-specific neutralizing antibody responses},
author = {Davide Pantarotto and Charalambos D Partidos and Johan Hoebeke and Fred Brown and Ed Kramer and Jean-Paul Briand and Sylviane Muller and Maurizio Prato and Alberto Bianco},
doi = {10.1016/j.chembiol.2003.09.011},
issn = {1074-5521},
year = {2003},
date = {2003-10-01},
journal = {Chemistry & Biology},
volume = {10},
number = {10},
pages = {961--966},
keywords = {Animals, Antibodies, Antigen-Antibody Reactions, carbon, Drug Delivery Systems, Epitopes, Foot-and-Mouth Disease Virus, I2CT, Immunization, Mice, Monoclonal, Nanotubes, Neutralization Tests, Peptides, Team-Bianco, Vaccines, Viral},
pubstate = {published},
tppubtype = {article}
}
Rainaldi Mario, Lancelot Nathalie, Elbayed Karim, Raya Jesus, Piotto Martial, Briand Jean-Paul, Kaptein Bernard, Broxterman Quirinus B, Berkessel Albrecht, Formaggio Fernando, Toniolo Claudio, Bianco Alberto
Conformational analysis by HRMAS NMR spectroscopy of resin-bound homo-peptides from C(alpha)-methyl-leucine Article de journal
Dans: Organic & Biomolecular Chemistry, vol. 1, no. 11, p. 1835–1837, 2003, ISSN: 1477-0520.
Résumé | Liens | BibTeX | Étiquettes: biomolecular, I2CT, Leucine, Nuclear Magnetic Resonance, Oligopeptides, Protein Structure, Resins, Secondary, Synthetic, Team-Bianco
@article{rainaldi_conformational_2003,
title = {Conformational analysis by HRMAS NMR spectroscopy of resin-bound homo-peptides from C(alpha)-methyl-leucine},
author = {Mario Rainaldi and Nathalie Lancelot and Karim Elbayed and Jesus Raya and Martial Piotto and Jean-Paul Briand and Bernard Kaptein and Quirinus B Broxterman and Albrecht Berkessel and Fernando Formaggio and Claudio Toniolo and Alberto Bianco},
doi = {10.1039/b303193d},
issn = {1477-0520},
year = {2003},
date = {2003-06-01},
journal = {Organic & Biomolecular Chemistry},
volume = {1},
number = {11},
pages = {1835--1837},
abstract = {A series of [L-(alphaMe)Leu]n (n = 1-5) homo-peptides have been covalently linked to Tentagel and POEPOP resins and submitted to a conformational study using HRMAS NMR spectroscopy. Whereas the mono- and dipeptide are mainly fully-extended, stable 3(10)-helical structures are formed beginning from the trimer.},
keywords = {biomolecular, I2CT, Leucine, Nuclear Magnetic Resonance, Oligopeptides, Protein Structure, Resins, Secondary, Synthetic, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
A series of [L-(alphaMe)Leu]n (n = 1-5) homo-peptides have been covalently linked to Tentagel and POEPOP resins and submitted to a conformational study using HRMAS NMR spectroscopy. Whereas the mono- and dipeptide are mainly fully-extended, stable 3(10)-helical structures are formed beginning from the trimer.
Pantarotto Davide, Partidos Charalambos D, Graff Roland, Hoebeke Johan, Briand Jean-Paul, Prato Maurizio, Bianco Alberto
Synthesis, structural characterization, and immunological properties of carbon nanotubes functionalized with peptides Article de journal
Dans: Journal of the American Chemical Society, vol. 125, no. 20, p. 6160–6164, 2003, ISSN: 0002-7863.
Résumé | Liens | BibTeX | Étiquettes: B-Lymphocyte, biomolecular, Capsid Proteins, carbon, Chromatography, Epitopes, Foot-and-Mouth Disease Virus, High Pressure Liquid, I2CT, nanotechnology, Nanotubes, Nuclear Magnetic Resonance, Peptide Fragments, Team-Bianco
@article{pantarotto_synthesis_2003,
title = {Synthesis, structural characterization, and immunological properties of carbon nanotubes functionalized with peptides},
author = {Davide Pantarotto and Charalambos D Partidos and Roland Graff and Johan Hoebeke and Jean-Paul Briand and Maurizio Prato and Alberto Bianco},
doi = {10.1021/ja034342r},
issn = {0002-7863},
year = {2003},
date = {2003-05-01},
journal = {Journal of the American Chemical Society},
volume = {125},
number = {20},
pages = {6160--6164},
abstract = {Carbon nanotubes (NTs) are becoming highly attractive molecules for applications in medicinal chemistry. The main problem of insolubility in aqueous media has been solved by developing a synthetic protocol that allows highly water-soluble carbon NTs to be obtained. As a result, biologically active peptides can be easily linked through a stable covalent bond to carbon NTs. We have demonstrated that a bound peptide from the foot-and-mouth disease virus, corresponding to the 141-159 region of the viral envelope protein VP1, retained the structural integrity and was recognized by monoclonal and polyclonal antibodies. In addition, this peptide-NT conjugate is immunogenic, eliciting antibody responses of the right specificity. Such a system could be greatly advantageous for diagnostic purposes and could find future applications in vaccine delivery.},
keywords = {B-Lymphocyte, biomolecular, Capsid Proteins, carbon, Chromatography, Epitopes, Foot-and-Mouth Disease Virus, High Pressure Liquid, I2CT, nanotechnology, Nanotubes, Nuclear Magnetic Resonance, Peptide Fragments, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Carbon nanotubes (NTs) are becoming highly attractive molecules for applications in medicinal chemistry. The main problem of insolubility in aqueous media has been solved by developing a synthetic protocol that allows highly water-soluble carbon NTs to be obtained. As a result, biologically active peptides can be easily linked through a stable covalent bond to carbon NTs. We have demonstrated that a bound peptide from the foot-and-mouth disease virus, corresponding to the 141-159 region of the viral envelope protein VP1, retained the structural integrity and was recognized by monoclonal and polyclonal antibodies. In addition, this peptide-NT conjugate is immunogenic, eliciting antibody responses of the right specificity. Such a system could be greatly advantageous for diagnostic purposes and could find future applications in vaccine delivery.
Lancelot Nathalie, Elbayed Karim, Raya Jésus, Piotto Martial, Briand Jean-Paul, Formaggio Fernando, Toniolo Claudio, Bianco Alberto
Characterization of the 310-helix in model peptides by HRMAS NMR spectroscopy Article de journal
Dans: Chemistry (Weinheim an Der Bergstrasse, Germany), vol. 9, no. 6, p. 1317–1323, 2003, ISSN: 0947-6539.
Résumé | Liens | BibTeX | Étiquettes: biomolecular, Fourier Transform Infrared, I2CT, Nuclear Magnetic Resonance, Peptides, Protein Conformation, spectroscopy, Team-Bianco
@article{lancelot_characterization_2003,
title = {Characterization of the 310-helix in model peptides by HRMAS NMR spectroscopy},
author = {Nathalie Lancelot and Karim Elbayed and Jésus Raya and Martial Piotto and Jean-Paul Briand and Fernando Formaggio and Claudio Toniolo and Alberto Bianco},
doi = {10.1002/chem.200390151},
issn = {0947-6539},
year = {2003},
date = {2003-03-01},
journal = {Chemistry (Weinheim an Der Bergstrasse, Germany)},
volume = {9},
number = {6},
pages = {1317--1323},
abstract = {A tetra- and a hepta-homopeptide from the C(alpha)-tetrasubstituted Aib (alpha-aminoisobutyric acid) residue were covalently linked to the POEPOP resin by the fragment-condensation approach. The conformational preferences of the two model peptides were determined for the first time on a solid support by means of high-resolution magic angle spinning NMR spectroscopy. The results obtained indicate that the Aib homopeptides adopt a regular 3(10)-helical structure even when they are covalently bound to a polymeric matrix, and thus confirm the remarkable conformational stability of the peptides rich in this amino acid. An ATR-FTIR spectroscopic investigation, performed in parallel, also confirmed that these polymer-bound peptides do indeed adopt a helical conformation. The results of this study open the possibility to exploit the peptide-resin conjugates based on C(alpha)-tetrasubstituted alpha-amino acids as helpful, structurally organized templates in molecular recognition studies or as catalysts in asymmetric synthesis.},
keywords = {biomolecular, Fourier Transform Infrared, I2CT, Nuclear Magnetic Resonance, Peptides, Protein Conformation, spectroscopy, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
A tetra- and a hepta-homopeptide from the C(alpha)-tetrasubstituted Aib (alpha-aminoisobutyric acid) residue were covalently linked to the POEPOP resin by the fragment-condensation approach. The conformational preferences of the two model peptides were determined for the first time on a solid support by means of high-resolution magic angle spinning NMR spectroscopy. The results obtained indicate that the Aib homopeptides adopt a regular 3(10)-helical structure even when they are covalently bound to a polymeric matrix, and thus confirm the remarkable conformational stability of the peptides rich in this amino acid. An ATR-FTIR spectroscopic investigation, performed in parallel, also confirmed that these polymer-bound peptides do indeed adopt a helical conformation. The results of this study open the possibility to exploit the peptide-resin conjugates based on C(alpha)-tetrasubstituted alpha-amino acids as helpful, structurally organized templates in molecular recognition studies or as catalysts in asymmetric synthesis.
Bianco A, Prato M
Can Carbon Nanotubes be Considered Useful Tools for Biological Applications? Article de journal
Dans: Advanced Materials, vol. 15, no. 20, p. 1765–1768, 2003, ISSN: 1521-4095.
Résumé | Liens | BibTeX | Étiquettes: Carbon nanotubes, Functionalization, I2CT, Team-Bianco
@article{bianco_can_2003,
title = {Can Carbon Nanotubes be Considered Useful Tools for Biological Applications?},
author = {A Bianco and M Prato},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/adma.200301646},
doi = {10.1002/adma.200301646},
issn = {1521-4095},
year = {2003},
date = {2003-01-01},
urldate = {2020-03-31},
journal = {Advanced Materials},
volume = {15},
number = {20},
pages = {1765--1768},
abstract = {Carbon nanotubes can be made soluble in both organic solvents and in aqueous solutions by organic functionalization. In particular, soluble carbon nanotubes can be further derivatized by coupling with amino acids and bioactive peptides. Immobilization of peptides to the external walls of carbon nanotubes may find interesting applications in diagnostics, vaccine and drug delivery, or multipresentation of bioactive molecules.},
keywords = {Carbon nanotubes, Functionalization, I2CT, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Carbon nanotubes can be made soluble in both organic solvents and in aqueous solutions by organic functionalization. In particular, soluble carbon nanotubes can be further derivatized by coupling with amino acids and bioactive peptides. Immobilization of peptides to the external walls of carbon nanotubes may find interesting applications in diagnostics, vaccine and drug delivery, or multipresentation of bioactive molecules.
2002
Georgakilas Vasilios, Tagmatarchis Nikos, Pantarotto Davide, Bianco Alberto, Briand Jean-Paul, Prato Maurizio
Amino acid functionalisation of water soluble carbon nanotubes Article de journal
Dans: Chemical Communications (Cambridge, England), no. 24, p. 3050–3051, 2002, ISSN: 1359-7345.
Résumé | Liens | BibTeX | Étiquettes: Amino Acids, carbon, I2CT, Nanotubes, Solubility, Team-Bianco, water
@article{georgakilas_amino_2002,
title = {Amino acid functionalisation of water soluble carbon nanotubes},
author = {Vasilios Georgakilas and Nikos Tagmatarchis and Davide Pantarotto and Alberto Bianco and Jean-Paul Briand and Maurizio Prato},
doi = {10.1039/b209843a},
issn = {1359-7345},
year = {2002},
date = {2002-12-01},
journal = {Chemical Communications (Cambridge, England)},
number = {24},
pages = {3050--3051},
abstract = {High solubility of SWNTs and MWNTs in water is obtained by organic functionalisation; derivatisation with N-protected glycine is also easily achieved.},
keywords = {Amino Acids, carbon, I2CT, Nanotubes, Solubility, Team-Bianco, water},
pubstate = {published},
tppubtype = {article}
}
High solubility of SWNTs and MWNTs in water is obtained by organic functionalisation; derivatisation with N-protected glycine is also easily achieved.
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}
}
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.
Cohen W M, Bianco A, Connan F, Camoin L, Dalod M, Lauvau G, Ferriès E, Culmann-Penciolelli B, van Endert P M, Briand J P, Choppin J, Guillet J G
Dans: Journal of Virology, vol. 76, no. 20, p. 10219–10225, 2002, ISSN: 0022-538X, 1098-5514.
Résumé | Liens | BibTeX | Étiquettes: I2CT, Team-Bianco
@article{cohen_study_2002,
title = {Study of Antigen-Processing Steps Reveals Preferences Explaining Differential Biological Outcomes of Two HLA-A2-Restricted Immunodominant Epitopes from Human Immunodeficiency Virus Type 1},
author = {W M Cohen and A Bianco and F Connan and L Camoin and M Dalod and G Lauvau and E Ferriès and B Culmann-Penciolelli and P M van Endert and J P Briand and J Choppin and J G Guillet},
url = {https://jvi.asm.org/content/76/20/10219},
doi = {10.1128/JVI.76.20.10219-10225.2002},
issn = {0022-538X, 1098-5514},
year = {2002},
date = {2002-10-01},
urldate = {2020-03-31},
journal = {Journal of Virology},
volume = {76},
number = {20},
pages = {10219--10225},
abstract = {Cytotoxic T-lymphocyte (CTL) responses directed to different human immunodeficiency virus (HIV) epitopes vary in their protective efficacy. In particular, HIV-infected cells are much more sensitive to lysis by anti-Gag/p17(77-85)/HLA-A2 than to that by anti-polymerase/RT(476-484)/HLA-A2 CTL, because of a higher density of p17(77-85) complexes. This report describes multiple processing steps favoring the generation of p17(77-85) complexes: (i) the exact COOH-terminal cleavage of epitopes by cellular proteases occurred faster and more frequently for p17(77-85) than for RT(476-484), and (ii) the binding efficiency of the transporter associated with antigen processing was greater for p17(77-85) precursors than for the RT(476-484) epitope. Surprisingly, these peptides, which differed markedly in their antigenicity, displayed qualitatively and quantitatively similar immunogenicity, suggesting differences in the mechanisms governing these phenomena. Here, we discuss the mechanisms responsible for such differences.},
keywords = {I2CT, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Cytotoxic T-lymphocyte (CTL) responses directed to different human immunodeficiency virus (HIV) epitopes vary in their protective efficacy. In particular, HIV-infected cells are much more sensitive to lysis by anti-Gag/p17(77-85)/HLA-A2 than to that by anti-polymerase/RT(476-484)/HLA-A2 CTL, because of a higher density of p17(77-85) complexes. This report describes multiple processing steps favoring the generation of p17(77-85) complexes: (i) the exact COOH-terminal cleavage of epitopes by cellular proteases occurred faster and more frequently for p17(77-85) than for RT(476-484), and (ii) the binding efficiency of the transporter associated with antigen processing was greater for p17(77-85) precursors than for the RT(476-484) epitope. Surprisingly, these peptides, which differed markedly in their antigenicity, displayed qualitatively and quantitatively similar immunogenicity, suggesting differences in the mechanisms governing these phenomena. Here, we discuss the mechanisms responsible for such differences.
Nisole Sébastien, Said Elias A, Mische Claudia, Prevost Marie-Christine, Krust Bernard, Bouvet Philippe, Bianco Alberto, Briand Jean-Paul, Hovanessian Ara G
The Anti-HIV Pentameric Pseudopeptide HB-19 Binds the C-terminal End of Nucleolin and Prevents Anchorage of Virus Particles in the Plasma Membrane of Target Cells Article de journal
Dans: Journal of Biological Chemistry, vol. 277, no. 23, p. 20877–20886, 2002, ISSN: 0021-9258, 1083-351X.
Résumé | Liens | BibTeX | Étiquettes: I2CT, Team-Bianco
@article{nisole_anti-hiv_2002,
title = {The Anti-HIV Pentameric Pseudopeptide HB-19 Binds the C-terminal End of Nucleolin and Prevents Anchorage of Virus Particles in the Plasma Membrane of Target Cells},
author = {Sébastien Nisole and Elias A Said and Claudia Mische and Marie-Christine Prevost and Bernard Krust and Philippe Bouvet and Alberto Bianco and Jean-Paul Briand and Ara G Hovanessian},
url = {http://www.jbc.org/content/277/23/20877},
doi = {10.1074/jbc.M110024200},
issn = {0021-9258, 1083-351X},
year = {2002},
date = {2002-07-01},
urldate = {2020-03-31},
journal = {Journal of Biological Chemistry},
volume = {277},
number = {23},
pages = {20877--20886},
abstract = {The multivalent pseudopeptide HB-19 that binds the cell-surface-expressed nucleolin is a potent inhibitor of human immunodeficiency virus (HIV) infection by blocking virus particle attachment and thus anchorage in the plasma membrane. We show that cross-linking of surface-bound HB-19A (like HB-19 but with a modified template) results in aggregation of HB-19A with surface nucleolin. Consistent with its specific action, HB-19A binding to different types of cells reaches saturation at concentrations that have been reported to result in inhibition of HIV infection. By using Chinese hamster ovary mutant cell lines, we confirm that the binding of HB-19A to surface nucleolin is independent of heparan and chondroitin sulfate proteoglycans. In vitro generated full-length nucleolin was found to bind HB-19A, whereas the N-terminal part containing the acidic amino acid stretches of nucleolin did not. The use of various deletion constructs of the C-terminal part of nucleolin then permitted the identification of the extreme C-terminal end of nucleolin, containing repeats of the amino acid motif, RGG, as the domain that binds HB-19A. Finally, a synthetic peptide corresponding to the last C-terminal 63 amino acids was able to inhibit HIV infection at the stage of HIV attachment to cells, thus suggesting that this domain could be functional in the HIV anchorage process.},
keywords = {I2CT, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
The multivalent pseudopeptide HB-19 that binds the cell-surface-expressed nucleolin is a potent inhibitor of human immunodeficiency virus (HIV) infection by blocking virus particle attachment and thus anchorage in the plasma membrane. We show that cross-linking of surface-bound HB-19A (like HB-19 but with a modified template) results in aggregation of HB-19A with surface nucleolin. Consistent with its specific action, HB-19A binding to different types of cells reaches saturation at concentrations that have been reported to result in inhibition of HIV infection. By using Chinese hamster ovary mutant cell lines, we confirm that the binding of HB-19A to surface nucleolin is independent of heparan and chondroitin sulfate proteoglycans. In vitro generated full-length nucleolin was found to bind HB-19A, whereas the N-terminal part containing the acidic amino acid stretches of nucleolin did not. The use of various deletion constructs of the C-terminal part of nucleolin then permitted the identification of the extreme C-terminal end of nucleolin, containing repeats of the amino acid motif, RGG, as the domain that binds HB-19A. Finally, a synthetic peptide corresponding to the last C-terminal 63 amino acids was able to inhibit HIV infection at the stage of HIV attachment to cells, thus suggesting that this domain could be functional in the HIV anchorage process.
Raya Jésus, Bianco Alberto, Furrer Julien, Briand Jean-Paul, Piotto Martial, Elbayed Karim
Proton dipolar recoupling in resin-bound peptides under high-resolution magic angle spinning Article de journal
Dans: Journal of Magnetic Resonance (San Diego, Calif.: 1997), vol. 157, no. 1, p. 43–51, 2002, ISSN: 1090-7807.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence, biomolecular, Foot-and-Mouth Disease Virus, I2CT, Nuclear Magnetic Resonance, Peptides, Plant, Resins, Team-Bianco
@article{raya_proton_2002,
title = {Proton dipolar recoupling in resin-bound peptides under high-resolution magic angle spinning},
author = {Jésus Raya and Alberto Bianco and Julien Furrer and Jean-Paul Briand and Martial Piotto and Karim Elbayed},
doi = {10.1006/jmre.2002.2573},
issn = {1090-7807},
year = {2002},
date = {2002-07-01},
journal = {Journal of Magnetic Resonance (San Diego, Calif.: 1997)},
volume = {157},
number = {1},
pages = {43--51},
abstract = {Rotational resonance and radiofrequency-driven dipolar recoupling (RFDR) experiments have been used to recover the weak proton dipolar interaction present in peptides bound to swollen resins spun at the magic angle. The intensity of the correlation peaks obtained using these sequences is shown to be significantly stronger than the one obtained using the classical NOESY experiment. In addition, it is found that during the relatively long mixing times required to transfer magnetization in such soft materials, the RFDR sequence also achieves magnetization transfer via the scalar J-coupling.},
keywords = {Amino Acid Sequence, biomolecular, Foot-and-Mouth Disease Virus, I2CT, Nuclear Magnetic Resonance, Peptides, Plant, Resins, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Rotational resonance and radiofrequency-driven dipolar recoupling (RFDR) experiments have been used to recover the weak proton dipolar interaction present in peptides bound to swollen resins spun at the magic angle. The intensity of the correlation peaks obtained using these sequences is shown to be significantly stronger than the one obtained using the classical NOESY experiment. In addition, it is found that during the relatively long mixing times required to transfer magnetization in such soft materials, the RFDR sequence also achieves magnetization transfer via the scalar J-coupling.
Furrer Julien, Elbayed Karim, Bourdonneau Maryse, Raya Jésus, Limal David, Bianco Alberto, Piotto Martial
Dynamic and magnetic susceptibility effects on the MAS NMR linewidth of a tetrapeptide bound to different resins Article de journal
Dans: Magnetic Resonance in Chemistry, vol. 40, no. 2, p. 123–132, 2002, ISSN: 1097-458X.
Résumé | Liens | BibTeX | Étiquettes: 13C NMR, 1H NMR, high-resolution magic angle spinning, I2CT, magnetic susceptibility, NMR, relaxation, solid-phase peptide synthesis, Team-Bianco
@article{furrer_dynamic_2002,
title = {Dynamic and magnetic susceptibility effects on the MAS NMR linewidth of a tetrapeptide bound to different resins},
author = {Julien Furrer and Karim Elbayed and Maryse Bourdonneau and Jésus Raya and David Limal and Alberto Bianco and Martial Piotto},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/mrc.970},
doi = {10.1002/mrc.970},
issn = {1097-458X},
year = {2002},
date = {2002-01-01},
urldate = {2020-03-31},
journal = {Magnetic Resonance in Chemistry},
volume = {40},
number = {2},
pages = {123--132},
abstract = {Under magic angle spinning, the NMR spectrum of the tetrapeptide Ala-Ile-Gly-Met bound to a Wang resin, and swollen in DMF, exhibits proton and carbon linewidths that are sharp enough to allow the complete characterization of the peptide using classical liquid-state NMR methods. The proton linewidths of the bound peptide remain, however, about three times larger than those of the free peptide in solution. The residual NMR linewidth originates essentially from incompletely averaged magnetic susceptibility effects due to the Wang resin. Replacing the aromatic Wang resin with a PEGA or POEPOP resin removes this effect. To investigate the contribution to line broadening of the peptide dynamics, relaxation studies were performed on the peptide bound to Wang and POEPOP resins. Copyright © 2001 John Wiley & Sons, Ltd.},
keywords = {13C NMR, 1H NMR, high-resolution magic angle spinning, I2CT, magnetic susceptibility, NMR, relaxation, solid-phase peptide synthesis, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Under magic angle spinning, the NMR spectrum of the tetrapeptide Ala-Ile-Gly-Met bound to a Wang resin, and swollen in DMF, exhibits proton and carbon linewidths that are sharp enough to allow the complete characterization of the peptide using classical liquid-state NMR methods. The proton linewidths of the bound peptide remain, however, about three times larger than those of the free peptide in solution. The residual NMR linewidth originates essentially from incompletely averaged magnetic susceptibility effects due to the Wang resin. Replacing the aromatic Wang resin with a PEGA or POEPOP resin removes this effect. To investigate the contribution to line broadening of the peptide dynamics, relaxation studies were performed on the peptide bound to Wang and POEPOP resins. Copyright © 2001 John Wiley & Sons, Ltd.
2001
Choppin Jeannine, Cohen William, Bianco Alberto, Briand Jean-Paul, Connan Francine, Dalod Marc, Guillet Jean-Gérard
Characteristics of HIV-1 Nef Regions Containing Multiple CD8+ Ŧ Cell Epitopes: Wealth of HLA-Binding Motifs and Sensitivity to Proteasome Degradation Article de journal
Dans: The Journal of Immunology, vol. 166, no. 10, p. 6164–6169, 2001, ISSN: 0022-1767, 1550-6606.
Résumé | Liens | BibTeX | Étiquettes: I2CT, Team-Bianco
@article{choppin_characteristics_2001,
title = {Characteristics of HIV-1 Nef Regions Containing Multiple CD8+ Ŧ Cell Epitopes: Wealth of HLA-Binding Motifs and Sensitivity to Proteasome Degradation},
author = {Jeannine Choppin and William Cohen and Alberto Bianco and Jean-Paul Briand and Francine Connan and Marc Dalod and Jean-Gérard Guillet},
url = {https://www.jimmunol.org/content/166/10/6164},
doi = {10.4049/jimmunol.166.10.6164},
issn = {0022-1767, 1550-6606},
year = {2001},
date = {2001-05-01},
urldate = {2020-03-31},
journal = {The Journal of Immunology},
volume = {166},
number = {10},
pages = {6164--6169},
abstract = {First and foremost among the many factors that influence epitope presentation are the degradation of Ag, which results in peptide liberation, and the presence of HLA class I molecules able to present the peptides to T lymphocytes. To define the regions of HIV-1 Nef that can provide multiple T cell epitopes, we analyzed the Nef sequence and determined that there are 73 peptides containing 81 HLA-binding motifs. We tested the binding of these peptides to six common HLA molecules (HLA-A2, -A3, -A24, -B7, -B8, and -B35), and we showed that most of them were efficient binders (54% of motifs), especially peptides associating with HLA-A3, -B7/35, and -B8 molecules. Nef peptides most frequently recognized by T cells of HIV-1-infected individuals were 90–97, 135–143, 71–81, 77–85, 90–100, 73–82, and 128–137. The frequency of T cell recognition was not directly related to the strength of peptide-HLA binding. The generation of Nef epitopes is crucial; therefore, we investigated the digestion by the 20S proteasome of a large peptide, Nef66–100. This fragment was efficiently cleaved, and NH2-terminally extended precursors of epitope 71–81 were recognized by T cells of an HIV-1-infected individual. These results suggest that a high frequency of T cell recognition may depend on proteasome cleavage.},
keywords = {I2CT, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
First and foremost among the many factors that influence epitope presentation are the degradation of Ag, which results in peptide liberation, and the presence of HLA class I molecules able to present the peptides to T lymphocytes. To define the regions of HIV-1 Nef that can provide multiple T cell epitopes, we analyzed the Nef sequence and determined that there are 73 peptides containing 81 HLA-binding motifs. We tested the binding of these peptides to six common HLA molecules (HLA-A2, -A3, -A24, -B7, -B8, and -B35), and we showed that most of them were efficient binders (54% of motifs), especially peptides associating with HLA-A3, -B7/35, and -B8 molecules. Nef peptides most frequently recognized by T cells of HIV-1-infected individuals were 90–97, 135–143, 71–81, 77–85, 90–100, 73–82, and 128–137. The frequency of T cell recognition was not directly related to the strength of peptide-HLA binding. The generation of Nef epitopes is crucial; therefore, we investigated the digestion by the 20S proteasome of a large peptide, Nef66–100. This fragment was efficiently cleaved, and NH2-terminally extended precursors of epitope 71–81 were recognized by T cells of an HIV-1-infected individual. These results suggest that a high frequency of T cell recognition may depend on proteasome cleavage.
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}
}
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.
Piotto Martial, Bourdonneau Maryse, Furrer Julien, Bianco Alberto, Raya Jésus, Elbayed Karim
Destruction of Magnetization during TOCSY Experiments Performed under Magic Angle Spinning: Effect of Radial B1 Inhomogeneities Article de journal
Dans: Journal of Magnetic Resonance, vol. 149, no. 1, p. 114–118, 2001, ISSN: 1090-7807.
Résumé | Liens | BibTeX | Étiquettes: I2CT, Team-Bianco
@article{piotto_destruction_2001,
title = {Destruction of Magnetization during TOCSY Experiments Performed under Magic Angle Spinning: Effect of Radial B1 Inhomogeneities},
author = {Martial Piotto and Maryse Bourdonneau and Julien Furrer and Alberto Bianco and Jésus Raya and Karim Elbayed},
url = {http://www.sciencedirect.com/science/article/pii/S1090780701922876},
doi = {10.1006/jmre.2001.2287},
issn = {1090-7807},
year = {2001},
date = {2001-03-01},
urldate = {2020-03-31},
journal = {Journal of Magnetic Resonance},
volume = {149},
number = {1},
pages = {114--118},
abstract = {TOCSY experiments performed on liquid-like samples under magic angle spinning conditions can exhibit some very peculiar behavior. In the most extreme cases, an almost complete loss of magnetization is observed. The intensity of the effect depends essentially on the ratio of the radiofrequency field strength to the speed of rotation of the sample. It is shown in this study that the periodic modulation of the B1 field in the course of the sample rotation is responsible for this effect.},
keywords = {I2CT, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
TOCSY experiments performed on liquid-like samples under magic angle spinning conditions can exhibit some very peculiar behavior. In the most extreme cases, an almost complete loss of magnetization is observed. The intensity of the effect depends essentially on the ratio of the radiofrequency field strength to the speed of rotation of the sample. It is shown in this study that the periodic modulation of the B1 field in the course of the sample rotation is responsible for this effect.
Furrer J, Piotto M, Bourdonneau M, Limal D, Guichard G, Elbayed K, Raya J, Briand J P, Bianco A
Evidence of secondary structure by high-resolution magic angle spinning NMR spectroscopy of a bioactive peptide bound to different solid supports Article de journal
Dans: Journal of the American Chemical Society, vol. 123, no. 18, p. 4130–4138, 2001, ISSN: 0002-7863.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence, biomolecular, Capsid, Capsid Proteins, Epitopes, I2CT, Molecular Sequence Data, Nuclear Magnetic Resonance, Peptide Fragments, Plant, Protein Structure, Resins, Secondary, Solvents, Team-Bianco
@article{furrer_evidence_2001,
title = {Evidence of secondary structure by high-resolution magic angle spinning NMR spectroscopy of a bioactive peptide bound to different solid supports},
author = {J Furrer and M Piotto and M Bourdonneau and D Limal and G Guichard and K Elbayed and J Raya and J P Briand and A Bianco},
doi = {10.1021/ja003566w},
issn = {0002-7863},
year = {2001},
date = {2001-01-01},
journal = {Journal of the American Chemical Society},
volume = {123},
number = {18},
pages = {4130--4138},
abstract = {The structure of the 19-amino acid peptide epitope, corresponding to the 141-159 sequence of capsid viral protein VP1 of foot-and-mouth disease virus (FMDV), bound to three different resins, namely, polystyrene-MBHA, PEGA, and POEPOP, has been determined by high-resolution magic angle spinning (HRMAS) NMR spectroscopy. A combination of homonuclear and heteronuclear bidimensional experiments was used for the complete peptide resonance assignment and the qualitative characterization of the peptide folding. The influence of the chemicophysical nature of the different polymers on the secondary structure of the covalently attached FMDV peptide was studied in detail. In the case of polystyrene-MBHA and polyacrylamide-PEGA resins, the analysis of the 2D spectra was hampered by missing signals and extensive overlaps, and only a propensity toward a peptide secondary structure could be derived from the assigned NOE correlations. When the FMDV peptide was linked to the polyoxyethylene-based POEPOP resin, it was found to adopt in dimethylformamide a helical conformation encompassing the C-terminal domain from residues 152 to 159. This conformation is very close to that of the free peptide previously analyzed in 2,2,2-trifluoroethanol. Our study clearly demonstrates that a regular helical structure can be adopted by a resin-bound bioactive peptide. Moreover, a change in the folding was observed when the same peptide-POEPOP conjugate was swollen in aqueous solution, displaying the same conformational features as the free peptide in water. The possibility of studying solid-supported ordered secondary structures by the HRMAS NMR technique in a wide range of solvents can be extended either to other biologically relevant peptides and proteins or to new synthetic oligomers.},
keywords = {Amino Acid Sequence, biomolecular, Capsid, Capsid Proteins, Epitopes, I2CT, Molecular Sequence Data, Nuclear Magnetic Resonance, Peptide Fragments, Plant, Protein Structure, Resins, Secondary, Solvents, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
The structure of the 19-amino acid peptide epitope, corresponding to the 141-159 sequence of capsid viral protein VP1 of foot-and-mouth disease virus (FMDV), bound to three different resins, namely, polystyrene-MBHA, PEGA, and POEPOP, has been determined by high-resolution magic angle spinning (HRMAS) NMR spectroscopy. A combination of homonuclear and heteronuclear bidimensional experiments was used for the complete peptide resonance assignment and the qualitative characterization of the peptide folding. The influence of the chemicophysical nature of the different polymers on the secondary structure of the covalently attached FMDV peptide was studied in detail. In the case of polystyrene-MBHA and polyacrylamide-PEGA resins, the analysis of the 2D spectra was hampered by missing signals and extensive overlaps, and only a propensity toward a peptide secondary structure could be derived from the assigned NOE correlations. When the FMDV peptide was linked to the polyoxyethylene-based POEPOP resin, it was found to adopt in dimethylformamide a helical conformation encompassing the C-terminal domain from residues 152 to 159. This conformation is very close to that of the free peptide previously analyzed in 2,2,2-trifluoroethanol. Our study clearly demonstrates that a regular helical structure can be adopted by a resin-bound bioactive peptide. Moreover, a change in the folding was observed when the same peptide-POEPOP conjugate was swollen in aqueous solution, displaying the same conformational features as the free peptide in water. The possibility of studying solid-supported ordered secondary structures by the HRMAS NMR technique in a wide range of solvents can be extended either to other biologically relevant peptides and proteins or to new synthetic oligomers.
2000
Bianco Alberto, Furrer Julien, Limal David, Guichard Gilles, Elbayed Karim, Raya Jésus, Piotto Martial, Briand Jean-Paul
Multistep Synthesis of 2,5-Diketopiperazines on Different Solid Supports Monitored by High Resolution Magic Angle Spinning NMR Spectroscopy Article de journal
Dans: Journal of Combinatorial Chemistry, vol. 2, no. 6, p. 681–690, 2000, ISSN: 1520-4766.
Résumé | Liens | BibTeX | Étiquettes: I2CT, Team-Bianco
@article{bianco_multistep_2000,
title = {Multistep Synthesis of 2,5-Diketopiperazines on Different Solid Supports Monitored by High Resolution Magic Angle Spinning NMR Spectroscopy},
author = {Alberto Bianco and Julien Furrer and David Limal and Gilles Guichard and Karim Elbayed and Jésus Raya and Martial Piotto and Jean-Paul Briand},
url = {https://doi.org/10.1021/cc0000489},
doi = {10.1021/cc0000489},
issn = {1520-4766},
year = {2000},
date = {2000-11-01},
urldate = {2020-03-31},
journal = {Journal of Combinatorial Chemistry},
volume = {2},
number = {6},
pages = {681--690},
abstract = {The solid-phase synthesis of 2,5-diketopiperazines containing the trans-4-hydroxy-l-proline amino acid residue (Hyp) was performed on Ellman polystyrene, polyoxyethylene-polyoxypropylene (POEPOP), polystyrene-polyoxyethylene NovaSyn, and Wang resins, respectively. The reaction pathway allowed the introduction of different functional groups around the bicyclic scaffold in a combinatorial approach, and it generated mixtures of isomers. A detailed characterization of the single reaction steps by high resolution magic angle spinning (HRMAS) NMR spectroscopy was performed. The NMR spectral resolution of the resin-bound intermediates and final products was greatly influenced by the polymer matrix. The POEPOP resin permitted to obtain HRMAS NMR spectra with a resolution comparable with that of the spectra of the molecules in solution. Moreover, configurational and conformational isomers formed during the solid-phase reaction steps could be detected and easily assigned. Therefore, the combination of the HRMAS NMR technique with the use of nonaromatic resins may become an extremely powerful tool in solid-phase organic synthesis. This approach will allow the monitoring of multistep reactions and the conception of on-bead structural studies either on small molecules or on natural and/or synthetic oligomers.},
keywords = {I2CT, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
The solid-phase synthesis of 2,5-diketopiperazines containing the trans-4-hydroxy-l-proline amino acid residue (Hyp) was performed on Ellman polystyrene, polyoxyethylene-polyoxypropylene (POEPOP), polystyrene-polyoxyethylene NovaSyn, and Wang resins, respectively. The reaction pathway allowed the introduction of different functional groups around the bicyclic scaffold in a combinatorial approach, and it generated mixtures of isomers. A detailed characterization of the single reaction steps by high resolution magic angle spinning (HRMAS) NMR spectroscopy was performed. The NMR spectral resolution of the resin-bound intermediates and final products was greatly influenced by the polymer matrix. The POEPOP resin permitted to obtain HRMAS NMR spectra with a resolution comparable with that of the spectra of the molecules in solution. Moreover, configurational and conformational isomers formed during the solid-phase reaction steps could be detected and easily assigned. Therefore, the combination of the HRMAS NMR technique with the use of nonaromatic resins may become an extremely powerful tool in solid-phase organic synthesis. This approach will allow the monitoring of multistep reactions and the conception of on-bead structural studies either on small molecules or on natural and/or synthetic oligomers.
Bianco Alberto, Sonksen Carsten P, Roepstorff Peter, Briand Jean-Paul
Solid-Phase Synthesis and Structural Characterization of Highly Substituted Hydroxyproline-Based 2,5-Diketopiperazines Article de journal
Dans: The Journal of Organic Chemistry, vol. 65, no. 7, p. 2179–2187, 2000, ISSN: 0022-3263.
Résumé | Liens | BibTeX | Étiquettes: I2CT, Team-Bianco
@article{bianco_solid-phase_2000,
title = {Solid-Phase Synthesis and Structural Characterization of Highly Substituted Hydroxyproline-Based 2,5-Diketopiperazines},
author = {Alberto Bianco and Carsten P Sonksen and Peter Roepstorff and Jean-Paul Briand},
url = {https://doi.org/10.1021/jo991818+},
doi = {10.1021/jo991818+},
issn = {0022-3263},
year = {2000},
date = {2000-04-01},
urldate = {2020-03-31},
journal = {The Journal of Organic Chemistry},
volume = {65},
number = {7},
pages = {2179--2187},
abstract = {Two general solid-phase methods for the synthesis of a new class of 2,5-diketopiperazines (DKPs) containing the trans-4-hydroxy-l-proline amino acid residue (Hyp) have been developed. An N-protected hydroxyproline methyl ester was linked through the hydroxyl function to the Ellman resin. The synthesis procedures were conceived to enable a sequence of Hyp alkylation, Hyp N-acylation, cyclization, and amide bond alkylation. Up to three different centers of molecular diversity were introduced around the DKP scaffold. Highly functionalized bicyclic compounds were obtained in good yield and purity. The alkylation of hydroxyproline αCH was performed without control of the diastereoselectivity. During the final alkylation of the backbone, amide bond epimerization at the α-carbon atoms of the two amino acid residues was observed. The structures of representative DKPs were elucidated with multidimensional NMR experiments. The described reaction pathways can be applied to the identification of heterocyclic molecule inhibitors to diverse enzyme targets.},
keywords = {I2CT, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Two general solid-phase methods for the synthesis of a new class of 2,5-diketopiperazines (DKPs) containing the trans-4-hydroxy-l-proline amino acid residue (Hyp) have been developed. An N-protected hydroxyproline methyl ester was linked through the hydroxyl function to the Ellman resin. The synthesis procedures were conceived to enable a sequence of Hyp alkylation, Hyp N-acylation, cyclization, and amide bond alkylation. Up to three different centers of molecular diversity were introduced around the DKP scaffold. Highly functionalized bicyclic compounds were obtained in good yield and purity. The alkylation of hydroxyproline αCH was performed without control of the diastereoselectivity. During the final alkylation of the backbone, amide bond epimerization at the α-carbon atoms of the two amino acid residues was observed. The structures of representative DKPs were elucidated with multidimensional NMR experiments. The described reaction pathways can be applied to the identification of heterocyclic molecule inhibitors to diverse enzyme targets.
Nisole Sébastien, Krust Bernard, Dam Elisabeth, Bianco Alberto, Seddiki Nabila, Loaec Solen, Callebaut Christian, Guichard Gilles, Muller Sylviane, Briand J, Hovanessian Ara
The HB-19 pseudopeptide 5[Kψ(CH2N)PR]-TASP inhibits attachment of Ŧ lymphocyte- and macrophage-tropic HIV to permissive cells Article de journal
Dans: AIDS research and human retroviruses, vol. 16, p. 237–49, 2000.
Résumé | Liens | BibTeX | Étiquettes: I2CT, Team-Bianco
@article{nisole_hb-19_2000,
title = {The HB-19 pseudopeptide 5[Kψ(CH2N)PR]-TASP inhibits attachment of Ŧ lymphocyte- and macrophage-tropic HIV to permissive cells},
author = {Sébastien Nisole and Bernard Krust and Elisabeth Dam and Alberto Bianco and Nabila Seddiki and Solen Loaec and Christian Callebaut and Gilles Guichard and Sylviane Muller and J Briand and Ara Hovanessian},
doi = {10.1089/088922200309331},
year = {2000},
date = {2000-03-01},
journal = {AIDS research and human retroviruses},
volume = {16},
pages = {237--49},
abstract = {The HB-19 pseudopeptide 5[Kpsi(CH2N)PR]-TASP[psi(CH2N) indicating a reduced peptide bond], which binds the cell surface-expressed nucleolin, is a potent inhibitor of HIV infection. Here, by using primary T lymphocyte cultures and an experimental cell model to monitor HIV entry, we show that HB-19 inhibits in a dose-dependent manner both T lymphocyte- and macrophage-tropic HIV isolates. Similar positively charged control pseudopeptides have no effect on HIV infection even at high concentrations. These observations, and the fact that HB-19 has no effect on SIV-mac and HIV-1 pseudotyped with VSV envelope glycoproteins, confirm the specific nature of this inhibitor against the entry process mediated by the HIV envelope glycoproteins. Finally, association of low doses of HB-19 with beta-chemokines or AZT results in an increased inhibitory effect on HIV infection. HB-19 has no inhibitory effect when added to cells a few hours after HIV entry. On the other hand, in HB-19-pretreated cells, the inhibitory effect persists for several hours, even after washing cells to remove away the unbound pseudopeptide. Under such conditions, the attachment of HIV particles to cells is inhibited as efficiently as by neutralizing monoclonal antibodies directed against the V3 loop. In view of its specific mode of action on various HIV isolates, HB-19 represents a potential anti-HIV drug.},
keywords = {I2CT, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
The HB-19 pseudopeptide 5[Kpsi(CH2N)PR]-TASP[psi(CH2N) indicating a reduced peptide bond], which binds the cell surface-expressed nucleolin, is a potent inhibitor of HIV infection. Here, by using primary T lymphocyte cultures and an experimental cell model to monitor HIV entry, we show that HB-19 inhibits in a dose-dependent manner both T lymphocyte- and macrophage-tropic HIV isolates. Similar positively charged control pseudopeptides have no effect on HIV infection even at high concentrations. These observations, and the fact that HB-19 has no effect on SIV-mac and HIV-1 pseudotyped with VSV envelope glycoproteins, confirm the specific nature of this inhibitor against the entry process mediated by the HIV envelope glycoproteins. Finally, association of low doses of HB-19 with beta-chemokines or AZT results in an increased inhibitory effect on HIV infection. HB-19 has no inhibitory effect when added to cells a few hours after HIV entry. On the other hand, in HB-19-pretreated cells, the inhibitory effect persists for several hours, even after washing cells to remove away the unbound pseudopeptide. Under such conditions, the attachment of HIV particles to cells is inhibited as efficiently as by neutralizing monoclonal antibodies directed against the V3 loop. In view of its specific mode of action on various HIV isolates, HB-19 represents a potential anti-HIV drug.
