Imagerie

@article{arosio_conjugation_2018,

title = {Conjugation of a GM3 lactone mimetic on carbon nanotubes enhances the related inhibition of melanoma-associated metastatic events},

author = {Paolo Arosio and Giuseppina Comito and Francesco Orsini and Alessandro Lascialfari and Paola Chiarugi and Cécilia Ménard-Moyon and Cristina Nativi and Barbara Richichi},

doi = {10.1039/c8ob01817k},

issn = {1477-0539},

year  = {2018},

date = {2018-01-01},

journal = {Organic & Biomolecular Chemistry},

volume = {16},

number = {33},

pages = {6086--6095},

abstract = {GM3-ganglioside is known to be involved in melanoma proliferation. In order to modulate metastatic-related events, we have functionalized multi-walled carbon nanotubes (MWCNTs) with multiple copies of a GM3-lactone mimetic. The MWCNTs proved to guarantee the appropriate spatial arrangement of the mimetic allowing a stronger inhibition of migration and invasiveness of human melanoma (A375) cells compared to other multivalent constructs reported before. In addition, the effect of the multivalent tubular conjugate on the inhibition of specific tyrosine kinases, which are associated with the ganglioside complexes within the membrane domains, was demonstrated. Finally, the short-term fate of the conjugate was assessed, for the first time, by means of the 1H NMR relaxometry technique by exploiting the signal arising from the CNTs.},

keywords = {Antineoplastic Agents, Biomimetic Materials, carbon, Cell Line, G(M3) Ganglioside, Humans, I2CT, Melanoma, Models, Molecular, Molecular Conformation, Nanotubes, Neoplasm Metastasis, Team-Bianco, tumor},

pubstate = {published},

tppubtype = {article}

}

@article{russier_oxidative_2011,

title = {Oxidative biodegradation of single- and multi-walled carbon nanotubes},

author = {Julie Russier and Cécilia Ménard-Moyon and Enrica Venturelli and Edmond Gravel and Gabriele Marcolongo and Moreno Meneghetti and Eric Doris and Alberto Bianco},

doi = {10.1039/c0nr00779j},

issn = {2040-3372},

year  = {2011},

date = {2011-03-01},

journal = {Nanoscale},

volume = {3},

number = {3},

pages = {893--896},

abstract = {In this study we compare the biodegradation of both single-walled (SWCNTs) and multi-walled carbon nanotubes (MWCNTs) using two different oxidative conditions. In particular, we demonstrate that oxidized multi-walled carbon nanotubes are highly degraded, although not to completeness when treated with horseradish peroxidase (HRP) in the presence of hydrogen peroxide.},

keywords = {Absorbable Implants, Biocompatible Materials, Body Fluids, carbon, Horseradish Peroxidase, Hydrogen Peroxide, I2CT, Macromolecular Substances, Materials Testing, Molecular Conformation, Nanotubes, Oxidation-Reduction, Particle Size, Surface Properties, Team-Bianco},

pubstate = {published},

tppubtype = {article}

}

@article{mishima_n-terminal_2009,

title = {The N-terminal domain of Drosophila Gram-negative binding protein 3 (GNBP3) defines a novel family of fungal pattern recognition receptors},

author = {Yumiko Mishima and Jessica Quintin and Vishukumar Aimanianda and Christine Kellenberger and Franck Coste and Cecile Clavaud and Charles Hetru and Jules A Hoffmann and Jean-Paul Latgé and Dominique Ferrandon and Alain Roussel},

doi = {10.1074/jbc.M109.034587},

issn = {1083-351X},

year  = {2009},

date = {2009-10-01},

journal = {J. Biol. Chem.},

volume = {284},

number = {42},

pages = {28687--28697},

abstract = {Gram-negative binding protein 3 (GNBP3), a pattern recognition receptor that circulates in the hemolymph of Drosophila, is responsible for sensing fungal infection and triggering Toll pathway activation. Here, we report that GNBP3 N-terminal domain binds to fungi upon identifying long chains of beta-1,3-glucans in the fungal cell wall as a major ligand. Interestingly, this domain fails to interact strongly with short oligosaccharides. The crystal structure of GNBP3-Nter reveals an immunoglobulin-like fold in which the glucan binding site is masked by a loop that is highly conserved among glucan-binding proteins identified in several insect orders. Structure-based mutagenesis experiments reveal an essential role for this occluding loop in discriminating between short and long polysaccharides. The displacement of the occluding loop is necessary for binding and could explain the specificity of the interaction with long chain structured polysaccharides. This represents a novel mechanism for beta-glucan recognition.},

keywords = {Animals, beta-Glucans, Bombyx, Carrier Proteins, Crystallography, ferrandon, Fungal Proteins, Hemolymph, hoffmann, ligands, M3i, Molecular Conformation, Mutagenesis, Polysaccharides, Protein Structure, Secondary, Tertiary, X-Ray},

pubstate = {published},

tppubtype = {article}

}

@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}

}