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}
}
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}
}
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}
}
Dimarcq Jean-Luc, Keppi E, Dunbar B, Lambert J, Reichhart Jean-Marc, Hoffmann Danièle, Rankine S M, Fothergill J E, Hoffmann Jules A
Insect immunity. Purification and characterization of a family of novel inducible antibacterial proteins from immunized larvae of the dipteran Phormia terranovae and complete amino-acid sequence of the predominant member, diptericin A Article de journal
Dans: Eur. J. Biochem., vol. 171, no. 1-2, p. 17–22, 1988, ISSN: 0014-2956.
Résumé | BibTeX | Étiquettes: Amino Acids, Animals, Anti-Bacterial Agents, Diptera, Escherichia coli, hoffmann, Insect Hormones, Insect Proteins, Isoelectric Point, Larva, M3i, reichhart
@article{dimarcq_insect_1988,
title = {Insect immunity. Purification and characterization of a family of novel inducible antibacterial proteins from immunized larvae of the dipteran Phormia terranovae and complete amino-acid sequence of the predominant member, diptericin A},
author = {Jean-Luc Dimarcq and E Keppi and B Dunbar and J Lambert and Jean-Marc Reichhart and Danièle Hoffmann and S M Rankine and J E Fothergill and Jules A Hoffmann},
issn = {0014-2956},
year = {1988},
date = {1988-01-01},
journal = {Eur. J. Biochem.},
volume = {171},
number = {1-2},
pages = {17--22},
abstract = {Injury or injection of live bacteria into third instar larvae of the dipteran insect Phormia terranovae results in the appearance in the haemolymph of at least five groups of heat-stable, more or less basic peptides with antibacterial activity against Escherichia coli. Three of these peptides have been purified. The amino acid sequence has been completely established for one of these and partially (first 40 residues from the N-terminus) for the two others. The sequences show marked homologies indicating that the three peptides belong to a common family. They are not related to other known antibacterial peptides from insects [lysozymes, cecropins (including sarcotoxin I) and attacins]. We propose the name of diptericins for this new family of antibiotic molecules.},
keywords = {Amino Acids, Animals, Anti-Bacterial Agents, Diptera, Escherichia coli, hoffmann, Insect Hormones, Insect Proteins, Isoelectric Point, Larva, M3i, reichhart},
pubstate = {published},
tppubtype = {article}
}
Debono M, Barnhart M, Carrell C B, Hoffmann Jules A, Occolowitz J L, Abbott B J, Fukuda D S, Hamill R L, Biemann K, Herlihy W C
A21978C, a complex of new acidic peptide antibiotics: isolation, chemistry, and mass spectral structure elucidation Article de journal
Dans: J. Antibiot., vol. 40, no. 6, p. 761–777, 1987, ISSN: 0021-8820.
Résumé | BibTeX | Étiquettes: Acylation, Amino Acids, Anti-Bacterial Agents, Chemical Phenomena, Chemistry, Chromatography, Cyclic, Fatty Acids, Gas Chromatography-Mass Spectrometry, High Pressure Liquid, hoffmann, Hydrolysis, M3i, Magnetic Resonance Spectroscopy, Mass Spectrometry, Molecular Conformation, Peptides, Spectrophotometry, Streptomyces
@article{debono_a21978c_1987,
title = {A21978C, a complex of new acidic peptide antibiotics: isolation, chemistry, and mass spectral structure elucidation},
author = {M Debono and M Barnhart and C B Carrell and Jules A Hoffmann and J L Occolowitz and B J Abbott and D S Fukuda and R L Hamill and K Biemann and W C Herlihy},
issn = {0021-8820},
year = {1987},
date = {1987-01-01},
journal = {J. Antibiot.},
volume = {40},
number = {6},
pages = {761--777},
abstract = {A21978C, produced by Streptomyces roseosporus, NRRL 11379, is a complex of new acidic lipopeptolide antibiotics which inhibits Gram-positive bacteria. HPLC separation of the various components from the purified complex resulted in the isolation of A21978C1, -C2 and -C3 (major components) and -C4, -C5, and -C0 (minor components). Each of these components was fermented with cultures of Actinoplanes utahensis (NRRL 12052) to give the identical inactive peptide ("A21978C nucleus") by removal of the fatty acid acyl groups from the N-terminus. This peptide was composed of 13 amino acids: L-kynurenine, L-threo-3-methylglutamic acid, L-asparagine, L-aspartic acid (3 residues), glycine (2 residues), L-tryptophan, L-ornithine, D-alanine, D-serine and L-threonine. The amino acid sequence was determined using a combination of the Edman degradation and gas chromatography mass spectrum (GC-MS) analysis of appropriately derivatized peptides obtained from partial hydrolysis. Each major component was shown to be acylated with a branched chain fatty acid at the N-terminus and the structure of this fatty acid was determined by 1H NMR and mass spectral methods. A structure for A21978C was assigned on the basis of this degradative and physico-chemical information.},
keywords = {Acylation, Amino Acids, Anti-Bacterial Agents, Chemical Phenomena, Chemistry, Chromatography, Cyclic, Fatty Acids, Gas Chromatography-Mass Spectrometry, High Pressure Liquid, hoffmann, Hydrolysis, M3i, Magnetic Resonance Spectroscopy, Mass Spectrometry, Molecular Conformation, Peptides, Spectrophotometry, Streptomyces},
pubstate = {published},
tppubtype = {article}
}