Marega Riccardo, Aroulmoji Vincent, Bergamin Massimo, Feruglio Luigi, Dinon Francesca, Bianco Alberto, Murano Erminio, Prato Maurizio
Two-dimensional diffusion-ordered NMR spectroscopy as a tool for monitoring functionalized carbon nanotube purification and composition Article de journal
Dans: ACS nano, vol. 4, no. 4, p. 2051–2058, 2010, ISSN: 1936-086X.
Résumé | Liens | BibTeX | Étiquettes: carbon, Diffusion, I2CT, Magnetic Resonance Spectroscopy, Nanotubes, Polyethylene Glycols, Solubility, Team-Bianco, Temperature, water
@article{marega_two-dimensional_2010,
title = {Two-dimensional diffusion-ordered NMR spectroscopy as a tool for monitoring functionalized carbon nanotube purification and composition},
author = {Riccardo Marega and Vincent Aroulmoji and Massimo Bergamin and Luigi Feruglio and Francesca Dinon and Alberto Bianco and Erminio Murano and Maurizio Prato},
doi = {10.1021/nn100257h},
issn = {1936-086X},
year = {2010},
date = {2010-04-01},
journal = {ACS nano},
volume = {4},
number = {4},
pages = {2051--2058},
abstract = {Functionalized carbon nanotube (CNT) derivatives are currently under thorough investigation in different biomedical investigations. In this field of research, the composition of sample either in terms of covalently attached or physisorbed moieties can greatly affect the observed results and hamper the comparison between different studies. Therefore, the availability of a fast and reliable analytical technique to assess both the type of interaction (covalent vs noncovalent) and the composition of CNT conjugates is of great importance. Here we describe that the two-dimensional diffusion-ordered (DOSY) NMR spectroscopy is extremely useful to discriminate between conjugated and unconjugated polyethylene glycol groups in samples obtained by condensation with oxidized single-walled carbon nanotubes (SWNTs). This fast and nondestructive technique allows us to follow the removal of unconjugated polyethylene glycol chains during the purification. In particular, DOSY analysis reveal that about 1/3 (wt %) of the polyethylene glycol used for the condensation remained physisorbed to functionalized SWNTs after dialysis. Complete elimination of physisorbed polyethylene glycol was achieved using diafiltration.},
keywords = {carbon, Diffusion, I2CT, Magnetic Resonance Spectroscopy, Nanotubes, Polyethylene Glycols, Solubility, Team-Bianco, Temperature, water},
pubstate = {published},
tppubtype = {article}
}
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}
}
Green Clare, Brown Gemma, Dafforn Timothy R, Reichhart Jean-Marc, Morley Terri, Lomas David A, Gubb David
Drosophila necrotic mutations mirror disease-associated variants of human serpins Article de journal
Dans: Development, vol. 130, no. 7, p. 1473–1478, 2003, ISSN: 0950-1991.
Résumé | BibTeX | Étiquettes: Animals, Humans, M3i, Necrosis, reichhart, Serpins, Temperature, Urea
@article{green_drosophila_2003,
title = {Drosophila necrotic mutations mirror disease-associated variants of human serpins},
author = {Clare Green and Gemma Brown and Timothy R Dafforn and Jean-Marc Reichhart and Terri Morley and David A Lomas and David Gubb},
issn = {0950-1991},
year = {2003},
date = {2003-04-01},
journal = {Development},
volume = {130},
number = {7},
pages = {1473--1478},
abstract = {Polymerization of members of the serpin superfamily underlies diseases as diverse as cirrhosis, angioedema, thrombosis and dementia. The Drosophila serpin Necrotic controls the innate immune response and is homologous to human alpha(1)-antitrypsin. We show that necrotic mutations that are identical to the Z-deficiency variant of alpha(1)-antitrypsin form urea-stable polymers in vivo. These necrotic mutations are temperature sensitive, which is in keeping with the temperature-dependent polymerization of serpins in vitro and the role of childhood fevers in exacerbating liver disease in Z alpha-antitrypsin deficiency. In addition, we identify two nec mutations homologous to an antithrombin point mutation that is responsible for neonatal thrombosis. Transgenic flies carrying an StextgreaterF amino-acid substitution equivalent to that found in Siiyama-variant antitrypsin (nec(StextgreaterF.UAS)) fail to complement nec-null mutations and demonstrate a dominant temperature-dependent inactivation of the wild-type nec allele. Taken together, these data establish Drosophila as a powerful system to study serpin polymerization in vivo.},
keywords = {Animals, Humans, M3i, Necrosis, reichhart, Serpins, Temperature, Urea},
pubstate = {published},
tppubtype = {article}
}
Salah R. Ben, Zouari N., Reinbolt J., Mejdoub H.
Purification of turkey pancreatic phospholipase A2 Article de journal
Dans: Biosci Biotechnol Biochem, vol. 67, no. 10, p. 2139-44, 2003, (0916-8451 Journal Article).
Résumé | BibTeX | Étiquettes: *Turkeys, &, A/*isolation, Acid, acids, Amino, Ammonium, and, Animals, Bile, Calcium, Chromatography, Concentration, Data, Hydrogen-Ion, Molecular, Pancreas/*enzymology, Phospholipases, purification, Salts, Sequence, Sulfate, Temperature, Weight
@article{,
title = {Purification of turkey pancreatic phospholipase A2},
author = { R. Ben Salah and N. Zouari and J. Reinbolt and H. Mejdoub},
year = {2003},
date = {2003-01-01},
journal = {Biosci Biotechnol Biochem},
volume = {67},
number = {10},
pages = {2139-44},
abstract = {Turkey pancreatic phospholipase (TPP) has been purified from delipidated pancreases. The purification included ammonium sulfate fractionation, acidic (pH 5) treatment, followed by sequencial column chromatographies on DEAE-cellulose, Sephadex G-75, and reverse phase high pressure liquid chromatography. The purified enzyme was found to be a monomeric protein with molecular mass of 14 kDa. The optimal activity was measured at pH 8 and 37 degrees C using egg yolk emulsion as substrate. Our results show that the enzyme (TPP) was not stable for 1 h at 60 degrees C, and that bile salt and Ca2+ were required for the expression of the purified enzyme. The sequence of the N-terminal amino acids of the purified enzyme shows a very close similarity between TPP and all other known pancreatic phospholipases.},
note = {0916-8451
Journal Article},
keywords = {*Turkeys, &, A/*isolation, Acid, acids, Amino, Ammonium, and, Animals, Bile, Calcium, Chromatography, Concentration, Data, Hydrogen-Ion, Molecular, Pancreas/*enzymology, Phospholipases, purification, Salts, Sequence, Sulfate, Temperature, Weight},
pubstate = {published},
tppubtype = {article}
}
Casimir J R, Iterbeke K, Nest W Van Den, Trescol-Biémont M C, Dumortier H, Muller S, Gerlier D, Rabourdin-Combe C, Tourwé D, Paris J
Conformational restriction of the Tyr53 side-chain in the decapeptide HE Article de journal
Dans: The Journal of Peptide Research: Official Journal of the American Peptide Society, vol. 56, no. 6, p. 398–408, 2000, ISSN: 1397-002X.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence, Animals, Antigen, Antigen-Presenting Cells, B-Lymphocytes, Chemical, Chickens, Dumortier, I2CT, Major Histocompatibility Complex, Mice, Models, Molecular Sequence Data, Muramidase, Peptide Biosynthesis, Peptides, Phenylalanine, Protein Binding, Protein Conformation, Receptors, T-Cell, Team-Dumortier, Temperature, Tyrosine
@article{casimir_conformational_2000,
title = {Conformational restriction of the Tyr53 side-chain in the decapeptide HE},
author = {J R Casimir and K Iterbeke and W Van Den Nest and M C Trescol-Biémont and H Dumortier and S Muller and D Gerlier and C Rabourdin-Combe and D Tourwé and J Paris},
doi = {10.1034/j.1399-3011.2000.00777.x},
issn = {1397-002X},
year = {2000},
date = {2000-12-01},
journal = {The Journal of Peptide Research: Official Journal of the American Peptide Society},
volume = {56},
number = {6},
pages = {398--408},
abstract = {A series of conformationally restricted analogs of the hen egg lysozyme (HEL) decapeptide 52-61 in which the conformationally flexible Tyr53 residue was replaced by several more constrained tyrosine and phenylalanine analogs was prepared. Among these tyrosine and phenylalanine analogs were 1,2,3,4-tetrahydro-7-hydroxyisoquinoline-3-carboxylic acid (Htc), 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid (Tic), 4-amino- 1,2,4,5-tetrahydro-8-hydroxy-2-benzazepine-3-one (Hba), 4-amino-1,2,4,5-tetrahydro-2-benzazepine-3-one (Aba), 2-amino-6-hydroxytetralin-2-carboxylic acid (Hat) and 2-amino-5-hydroxyindan-2-carboxylic acid (Hai) in which the rotations around Calpha-Cbeta and Cbeta-Cgamma were restricted because of cyclization of the side-chain to the backbone. Synthesis of Pht-Hba-Gly-OH using a modification of the Flynn and de Laszlo procedure is described. Analogs of beta-methyltyrosine (beta-MeTyr) in which the side-chains were biased to particular side-chain torsional angles because of substitution at the beta-hydrogens were also prepared. These analogs of HEL[52-61] peptide were tested for their ability to bind to the major histocompatibility complex class II I-Ak molecule and to be recognized in this context by two T-cell hybridomas, specific for the parent peptide HEL[52-61]. The data showed that the conformation and also the configuration of the Tyr53 residue influenced both the binding of the peptide to I-Ak and the recognition of the peptide/I-Ak complex by a T-cell receptor.},
keywords = {Amino Acid Sequence, Animals, Antigen, Antigen-Presenting Cells, B-Lymphocytes, Chemical, Chickens, Dumortier, I2CT, Major Histocompatibility Complex, Mice, Models, Molecular Sequence Data, Muramidase, Peptide Biosynthesis, Peptides, Phenylalanine, Protein Binding, Protein Conformation, Receptors, T-Cell, Team-Dumortier, Temperature, Tyrosine},
pubstate = {published},
tppubtype = {article}
}