Publications
2005
Bianco Alberto
Efficient solid-phase synthesis of fullero-peptides using Merrifield strategy Article de journal
Dans: Chemical Communications (Cambridge, England), no. 25, p. 3174–3176, 2005, ISSN: 1359-7345.
Résumé | Liens | BibTeX | Étiquettes: Chromatography, Fullerenes, High Pressure Liquid, I2CT, Mass Spectrometry, Peptides, Team-Bianco
@article{bianco_efficient_2005,
title = {Efficient solid-phase synthesis of fullero-peptides using Merrifield strategy},
author = {Alberto Bianco},
doi = {10.1039/b504659a},
issn = {1359-7345},
year = {2005},
date = {2005-07-01},
journal = {Chemical Communications (Cambridge, England)},
number = {25},
pages = {3174--3176},
abstract = {Boc-protected l-fulleropyrrolidino-glutamic acid was readily prepared and employed for the synthesis of fullerene-containing peptides using the solid-phase Boc chemistry developed by Merrifield.},
keywords = {Chromatography, Fullerenes, High Pressure Liquid, I2CT, Mass Spectrometry, Peptides, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
1996
Ehret-Sabatier L, Loew D, Goyffon M, Fehlbaum P, Hoffmann Jules A, van Dorsselaer A, Bulet Philippe
Characterization of novel cysteine-rich antimicrobial peptides from scorpion blood Article de journal
Dans: J. Biol. Chem., vol. 271, no. 47, p. 29537–29544, 1996, ISSN: 0021-9258.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Chromatography, Cysteine, Electron, Hemolymph, Hemolysis, High Pressure Liquid, hoffmann, M3i, Mass Spectrometry, Microscopy, Peptides, Scorpions
@article{ehret-sabatier_characterization_1996,
title = {Characterization of novel cysteine-rich antimicrobial peptides from scorpion blood},
author = {L Ehret-Sabatier and D Loew and M Goyffon and P Fehlbaum and Jules A Hoffmann and A van Dorsselaer and Philippe Bulet},
issn = {0021-9258},
year = {1996},
date = {1996-11-01},
journal = {J. Biol. Chem.},
volume = {271},
number = {47},
pages = {29537--29544},
abstract = {We have isolated, from the hemolymph of unchallenged scorpions of the species Androctonus australis, three distinct antimicrobial peptides, which we have fully characterized by Edman degradation, electrospray ionization mass spectrometry, and matrix-assisted laser desorption/ionization mass spectrometry. Two are novel molecules: (i) androctonin, a 25-residue peptide with two disulfide bridges, active against both bacteria (Gram-positive and Gram-negative) and fungi and showing marked sequence homology to tachyplesins and polyphemusins from horseshoe crabs; and (ii) buthinin, a 34-residue antibacterial (Gram-positive and Gram-negative) peptide with three disulfide bridges. The third peptide contains 37 residues and three disulfide bridges and clearly belongs to the family of anti-Gram-positive insect defensins. We have synthesized androctonin and explored its activity spectrum and mode of action.},
keywords = {Animals, Anti-Bacterial Agents, Chromatography, Cysteine, Electron, Hemolymph, Hemolysis, High Pressure Liquid, hoffmann, M3i, Mass Spectrometry, Microscopy, Peptides, Scorpions},
pubstate = {published},
tppubtype = {article}
}
Fehlbaum P, Bulet Philippe, Chernysh S, Briand J P, Roussel J P, Letellier L, Hetru Charles, Hoffmann Jules A
Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides Article de journal
Dans: Proc. Natl. Acad. Sci. U.S.A., vol. 93, no. 3, p. 1221–1225, 1996, ISSN: 0027-8424.
Résumé | BibTeX | Étiquettes: Amino Acid, Amphibian Proteins, Animals, Anti-Bacterial Agents, Anti-Infective Agents, Antimicrobial Cationic Peptides, Cyclic, Fungi, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemiptera, hoffmann, M3i, Mass Spectrometry, Microbial Sensitivity Tests, Peptides, Ranidae, Sequence Homology, Skin, Structure-Activity Relationship
@article{fehlbaum_structure-activity_1996,
title = {Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides},
author = {P Fehlbaum and Philippe Bulet and S Chernysh and J P Briand and J P Roussel and L Letellier and Charles Hetru and Jules A Hoffmann},
issn = {0027-8424},
year = {1996},
date = {1996-02-01},
journal = {Proc. Natl. Acad. Sci. U.S.A.},
volume = {93},
number = {3},
pages = {1221--1225},
abstract = {Immune challenge to the insect Podisus maculiventris induces synthesis of a 21-residue peptide with sequence homology to frog skin antimicrobial peptides of the brevinin family. The insect and frog peptides have in common a C-terminally located disulfide bridge delineating a cationic loop. The peptide is bactericidal and fungicidal, exhibiting the largest antimicrobial spectrum observed so far for an insect defense peptide. An all-D-enantiomer is nearly inactive against Gram-negative bacteria and some Gram-positive strains but is fully active against fungi and other Gram-positive bacteria, suggesting that more than one mechanism accounts for the antimicrobial activity of this peptide. Studies with truncated synthetic isoforms underline the role of the C-terminal loop and flanking residues for the activity of this molecule for which we propose the name thanatin.},
keywords = {Amino Acid, Amphibian Proteins, Animals, Anti-Bacterial Agents, Anti-Infective Agents, Antimicrobial Cationic Peptides, Cyclic, Fungi, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemiptera, hoffmann, M3i, Mass Spectrometry, Microbial Sensitivity Tests, Peptides, Ranidae, Sequence Homology, Skin, Structure-Activity Relationship},
pubstate = {published},
tppubtype = {article}
}
1995
Bulet Philippe, Hegy G, Lambert J, van Dorsselaer Alan, Hoffmann Jules A, Hetru Charles
Insect immunity. The inducible antibacterial peptide diptericin carries two O-glycans necessary for biological activity Article de journal
Dans: Biochemistry, vol. 34, no. 22, p. 7394–7400, 1995, ISSN: 0006-2960.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Carbohydrate Sequence, Carbohydrates, Diptera, Escherichia coli, Glycopeptides, Hemolymph, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mass Spectrometry, Plants, Trisaccharides
@article{bulet_insect_1995,
title = {Insect immunity. The inducible antibacterial peptide diptericin carries two O-glycans necessary for biological activity},
author = {Philippe Bulet and G Hegy and J Lambert and Alan van Dorsselaer and Jules A Hoffmann and Charles Hetru},
issn = {0006-2960},
year = {1995},
date = {1995-06-01},
journal = {Biochemistry},
volume = {34},
number = {22},
pages = {7394--7400},
abstract = {A bacterial challenge of larvae of the dipteran insect Phormia terranovae induces the rapid synthesis of diptericin, an antibacterial polypeptide, previously characterized at the amino acid level and indirectly by cDNA cloning studies. This 82-residue polypeptide consists of an N-terminal proline-rich domain and a central and C-terminal glycine-rich domain. Using liquid chromatography coupled to electrospray ionization-mass spectrometry, we demonstrate here that this molecule is more complex than anticipated and carries two O-substitutions on threonine residues, one in the proline-rich domain (residue 10) and one in the glycine-rich domain (residue 54). These substitutions consist of identical trisaccharides: glucose--textgreatergalactose--textgreaterN-acetylgalactosamine--textgreater(threonine). Treatment of diptericin with O-glycosidase, which selectively removes the substitutions without altering the polypeptide proper, abolishes the antibacterial activity, indicating that this posttranslational modification is essential for biological activity of the polypeptide. We also show that diptericin is posttranslationally modified by a C-terminal amidation.},
keywords = {Animals, Anti-Bacterial Agents, Carbohydrate Sequence, Carbohydrates, Diptera, Escherichia coli, Glycopeptides, Hemolymph, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mass Spectrometry, Plants, Trisaccharides},
pubstate = {published},
tppubtype = {article}
}
1992
Bulet Philippe, Cociancich S, Reuland M, Sauber F, Bischoff R, Hegy G, Dorsselaer Van A, Hetru Charles, Hoffmann Jules A
A novel insect defensin mediates the inducible antibacterial activity in larvae of the dragonfly Aeschna cyanea (Paleoptera, Odonata) Article de journal
Dans: Eur. J. Biochem., vol. 209, no. 3, p. 977–984, 1992, ISSN: 0014-2956.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Blood Bactericidal Activity, Blood Proteins, Defensins, Hemolymph, hoffmann, Insect Proteins, insects, Larva, M3i, Mass Spectrometry, Peptides
@article{bulet_novel_1992,
title = {A novel insect defensin mediates the inducible antibacterial activity in larvae of the dragonfly Aeschna cyanea (Paleoptera, Odonata)},
author = {Philippe Bulet and S Cociancich and M Reuland and F Sauber and R Bischoff and G Hegy and Van A Dorsselaer and Charles Hetru and Jules A Hoffmann},
issn = {0014-2956},
year = {1992},
date = {1992-11-01},
journal = {Eur. J. Biochem.},
volume = {209},
number = {3},
pages = {977--984},
abstract = {The injection of low doses of bacteria into the aquatic larvae of dragonflies (Aeschna cyanea, Odonata, Paleoptera) induces the appearance in their hemolymph of a potent antibacterial activity. We have isolated a 38-residue peptide from this hemolymph which is strongly active against Gram-positive bacteria and also shows activity against one of the Gram-negative bacteria which was tested. The peptide is a novel member of the insect defensin family of inducible antibacterial peptides, which had so far only been reported from the higher insect orders believed to have evolved 100 million years after the Paleoptera. Aeschna defensin is more potent than defensin from the dipteran Phormia, from which its structure differs in several interesting aspects, which are discussed in the paper.},
keywords = {Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Blood Bactericidal Activity, Blood Proteins, Defensins, Hemolymph, hoffmann, Insect Proteins, insects, Larva, M3i, Mass Spectrometry, Peptides},
pubstate = {published},
tppubtype = {article}
}
1991
Hetru Charles, Li K W, Bulet Philippe, Lagueux Marie, Hoffmann Jules A
Isolation and structural characterization of an insulin-related molecule, a predominant neuropeptide from Locusta migratoria Article de journal
Dans: Eur. J. Biochem., vol. 201, no. 2, p. 495–499, 1991, ISSN: 0014-2956.
Résumé | BibTeX | Étiquettes: Animals, Chromatography, DNA, Female, Grasshoppers, High Pressure Liquid, hoffmann, Insect Hormones, Insulin, M3i, Mass Spectrometry, Neuropeptides, Proinsulin, Protein Conformation
@article{hetru_isolation_1991,
title = {Isolation and structural characterization of an insulin-related molecule, a predominant neuropeptide from Locusta migratoria},
author = {Charles Hetru and K W Li and Philippe Bulet and Marie Lagueux and Jules A Hoffmann},
issn = {0014-2956},
year = {1991},
date = {1991-10-01},
journal = {Eur. J. Biochem.},
volume = {201},
number = {2},
pages = {495--499},
abstract = {Neurohaemal lobes of corpora cardiaca of Locusta migratoria are an established storage site for neurohormones produced by the neurosecretory cells of the brain. As previously reported [Hietter, H., Van Dorsselaer, A., Green, B., Denoroy, L., Hoffmann, J.A. & Luu, B. (1990) Eur. J. Biochem. 187, 241-247], the isolation and characterization of a novel 5-kDa peptide from these lobes served as the basis for oligonucleotide screening of cDNA libraries prepared from poly(A) RNA from neurosecretory cells of the central nervous system. From subsequent cDNA cloning studies [Lagueux, M., Lwoff, L., Meister, M., Goltzené, F. & Hoffmann, J.A. (1990) Eur. J. Biochem. 187, 249-254], the existence of a 145-residue precursor protein was deduced, which contained, in addition to the 5-kDa peptide, amino-acid sequences with homology to the A and B chains of an insulin-related peptide. In the present study we have isolated the native molecule from corpora cardiaca of Locusta and characterized, by Edman degradation and plasma-desorption mass spectrometry, the two chains as follows: A chain, Gly-Val-Phe-Asp-Glu-Cys-Cys-Arg-Lys-Ser-Cys-Ser-Ile-Ser-Glu-Leu-Gln-Thr- Tyr-Cys - Gly (Ile, isoleucine); B chain, Ser-Gly-Ala-Pro-Gln-Pro-Val-Ala-Arg-Tyr-Cys-Gly-Glu-Lys-Leu-Ser-Asn-Ala- Leu-Lys - Leu-Val-Cys-Arg-Gly-Asn-Tyr-Asn-Thr-Met-Phe. Taken in conjunction with the previous cloning studies, our data lead to a clear picture of the processing of Locusta preproinsulin. They indicate that locusta corpora cardiaca contain remarkably large amounts of one single insulin form, in contrast to multiple insulin isoforms of Bombyx mori, the only other insect species from which insulin-related peptides have been isolated and characterized [Nagasawa, H., Kataoka, H., Isogai, A., Tamura, S., Suzuki, A., Mizoguchi, A., Fujiwara, Y., Suzuki, A., Takahashi, S. & Ishizaki, H. (1986) Proc. Natl Acad. Sci. USA 83, 5840-5843].},
keywords = {Animals, Chromatography, DNA, Female, Grasshoppers, High Pressure Liquid, hoffmann, Insect Hormones, Insulin, M3i, Mass Spectrometry, Neuropeptides, Proinsulin, Protein Conformation},
pubstate = {published},
tppubtype = {article}
}
Lepage P, Bitsch F, Roecklin D, Keppi E, Dimarcq Jean-Luc, Reichhart Jean-Marc, Hoffmann Jules A, Roitsch C, Dorsselaer Van A
Determination of disulfide bridges in natural and recombinant insect defensin A Article de journal
Dans: Eur. J. Biochem., vol. 196, no. 3, p. 735–742, 1991, ISSN: 0014-2956.
Résumé | BibTeX | Étiquettes: Animals, Blood Proteins, Defensins, Diptera, Disulfides, Hemolymph, hoffmann, M3i, Mass Spectrometry, Recombinant Proteins, reichhart
@article{lepage_determination_1991,
title = {Determination of disulfide bridges in natural and recombinant insect defensin A},
author = {P Lepage and F Bitsch and D Roecklin and E Keppi and Jean-Luc Dimarcq and Jean-Marc Reichhart and Jules A Hoffmann and C Roitsch and Van A Dorsselaer},
issn = {0014-2956},
year = {1991},
date = {1991-01-01},
journal = {Eur. J. Biochem.},
volume = {196},
number = {3},
pages = {735--742},
abstract = {The primary-structure comparison of natural insect defensin A from Phormia terranovae and recombinant insect defensin A from Saccharomyces cerevisiae has been accomplished using a combination of Edman degradation and liquid secondary ion mass spectrometry. The natural and recombinant proteins have the same primary structure with identical disulfide-bond designations (formula; see text) as determined from the peptides obtained after thermolysin digestion. The combined use of Edman degradation and mass spectometry allowed the disulfide-bridge structure to be determined with a total of only 40 micrograms (9.9 nmol) natural peptide. Mass spectrometry provides a rapid means of disulfide-bridge verification, requiring not more than 20 micrograms recombinant insect defensin A, which is compatible with use in batch analysis.},
keywords = {Animals, Blood Proteins, Defensins, Diptera, Disulfides, Hemolymph, hoffmann, M3i, Mass Spectrometry, Recombinant Proteins, reichhart},
pubstate = {published},
tppubtype = {article}
}
1987
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}
}
1985
Hetru Charles, Luu B, Hoffmann Jules A
Ecdysone conjugates: isolation and identification Article de journal
Dans: Meth. Enzymol., vol. 111, p. 411–419, 1985, ISSN: 0076-6879.
BibTeX | Étiquettes: Animals, Bombyx, Chromatography, Ecdysone, Helix (Snails), High Pressure Liquid, hoffmann, Insect Hormones, M3i, Magnetic Resonance Spectroscopy, Mass Spectrometry, Spectrophotometry, Structure-Activity Relationship
@article{hetru_ecdysone_1985,
title = {Ecdysone conjugates: isolation and identification},
author = {Charles Hetru and B Luu and Jules A Hoffmann},
issn = {0076-6879},
year = {1985},
date = {1985-01-01},
journal = {Meth. Enzymol.},
volume = {111},
pages = {411--419},
keywords = {Animals, Bombyx, Chromatography, Ecdysone, Helix (Snails), High Pressure Liquid, hoffmann, Insect Hormones, M3i, Magnetic Resonance Spectroscopy, Mass Spectrometry, Spectrophotometry, Structure-Activity Relationship},
pubstate = {published},
tppubtype = {article}
}
1978
Hetru Charles, Lagueux Marie, Bang L, Hoffmann Jules A
Adult ovaries of Locusta migratoria contain the sequence of biosynthetic intermediates for ecdysone Article de journal
Dans: Life Sci., vol. 22, no. 23, p. 2141–2154, 1978, ISSN: 0024-3205.
BibTeX | Étiquettes: Animals, Chemical Phenomena, Chemistry, Cholesterol, Ecdysone, Female, Grasshoppers, hoffmann, M3i, Mass Spectrometry, Ovary, Ovum
@article{hetru_adult_1978,
title = {Adult ovaries of Locusta migratoria contain the sequence of biosynthetic intermediates for ecdysone},
author = {Charles Hetru and Marie Lagueux and L Bang and Jules A Hoffmann},
issn = {0024-3205},
year = {1978},
date = {1978-06-01},
journal = {Life Sci.},
volume = {22},
number = {23},
pages = {2141--2154},
keywords = {Animals, Chemical Phenomena, Chemistry, Cholesterol, Ecdysone, Female, Grasshoppers, hoffmann, M3i, Mass Spectrometry, Ovary, Ovum},
pubstate = {published},
tppubtype = {article}
}
1976
Bang L, Lagueux Marie, Hirn M, Hoffmann Jules A
Identification, by gas chromatography and mass spectrometry, of ecdysone synthesized in the ovaries of adult female Locusta migratoria (Insecta, Orthoptera) Article de journal
Dans: C.R. Hebd. Seances Acad. Sci., Ser. D, Sci. Nat., vol. 283, no. 9, p. 1081–1084, 1976.
Résumé | BibTeX | Étiquettes: Age Factors, Animals, Chromatography, Ecdysone, Female, Gas, Grasshoppers, hoffmann, M3i, Mass Spectrometry, Ovary
@article{bang_identification_1976,
title = {Identification, by gas chromatography and mass spectrometry, of ecdysone synthesized in the ovaries of adult female Locusta migratoria (Insecta, Orthoptera)},
author = {L Bang and Marie Lagueux and M Hirn and Jules A Hoffmann},
year = {1976},
date = {1976-10-01},
journal = {C.R. Hebd. Seances Acad. Sci., Ser. D, Sci. Nat.},
volume = {283},
number = {9},
pages = {1081--1084},
abstract = {Gas chromatographic analysis, coupled to mass spectrometry, demonstrates that the considerable amounts of ecdysteroids produced in the ovaries of female adults of Locusta migratoria at the end of each ovarian cycle, consist predominantly of ecdysone.},
keywords = {Age Factors, Animals, Chromatography, Ecdysone, Female, Gas, Grasshoppers, hoffmann, M3i, Mass Spectrometry, Ovary},
pubstate = {published},
tppubtype = {article}
}